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Journal articles on the topic 'OMP26'

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Published: 4 June 2021
Last updated: 4 February 2022

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1

Kyd, Jennelle M., and Allan W. Cripps. "Potential of a Novel Protein, OMP26, from Nontypeable Haemophilus influenzae To Enhance Pulmonary Clearance in a Rat Model." Infection and Immunity 66, no. 5 (May 1, 1998): 2272–78. http://dx.doi.org/10.1128/iai.66.5.2272-2278.1998.

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ABSTRACT A major outer membrane protein band of approximately 25 to 27 kDa is commonly observed in strains of Haemophilus influenzae. This study has investigated the potential of a 26-kDa protein (OMP26) from nontypeable H. influenzae (NTHI) as a vaccine candidate. OMP26 was used to immunize rats via intestinal Peyer’s patches, followed by an intratracheal boost. Immunization was found to significantly enhance bacterial clearance following pulmonary challenge with both the homologous NTHI strain and a different NTHI strain. Significant levels of anti-OMP26 were found in the serum and bronchoalveolar lavage from immunized rats, and isotypes of immunoglobulin G (IgG) were also measured in serum. Analysis of IgG isotypes present in serum following OMP26-immunization suggest that predominantly a T-helper 1-type response was induced. The OMP26 protein was amino-terminally sequenced and found to have no homology with the P5 of H. influenzae type b P5 or the fimbrin protein of NTHI, both can migrate upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis at similar molecular masses but OMP26 has 100% homology with a segment of the H. influenzae Rd genome. The results of this study suggest that OMP26 may be a suitable vaccine candidate against NTHI infection and warrants continued investigation and characterization.
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2

El-Adhami, Wafa, Jennelle M. Kyd, David A. Bastin, and Allan W. Cripps. "Characterization of the Gene Encoding a 26-Kilodalton Protein (OMP26) from Nontypeable Haemophilus influenzae and Immune Responses to the Recombinant Protein." Infection and Immunity 67, no. 4 (April 1, 1999): 1935–42. http://dx.doi.org/10.1128/iai.67.4.1935-1942.1999.

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ABSTRACT A 26-kDa protein (OMP26) isolated and purified from nontypeableHaemophilus influenzae (NTHI) strain 289 has been shown to enhance clearance of infection following pulmonary challenge with NTHI in rats. DNA sequence analysis revealed that it was 99% identical to a gene encoding a cell envelope protein of the H. influenzaeRd strain (TIGR accession no. HI0916). The deduced amino acid sequence revealed a hydrophilic polypeptide rich in basic amino acids. Restriction fragment length polymorphism analysis suggested that the OMP26 gene was relatively conserved among isolates of NTHI. Analysis of the deduced amino acid sequence of the OMP26 gene from 20 different isolates showed that similarity with NTHI-289 ranged from 96.5% (1 isolate) to 99.5% (14 isolates). Two recombinant forms of OMP26, a full length 28-kDa protein (equivalent to preprotein) and a 26-kDa protein lacking a 23-amino-acid leader peptide (equivalent to processed protein), were assessed in immunization studies for the ability to induce an immune response that would be as effective as the native protein in enhancing the clearance of NTHI following pulmonary challenge in rats. Immunization with the recombinant protein that included the leader peptide was more effective in enhancing pulmonary clearance, and it induced a better cell-mediated response and higher titers of systemic and mucosal antibody. This study has characterized a 26-kDa protein from NTHI that shows significant potential as a vaccine candidate.
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3

Kyd, Jennelle M., Allan W. Cripps, Laura A. Novotny, and Lauren O. Bakaletz. "Efficacy of the 26-Kilodalton Outer Membrane Protein and Two P5 Fimbrin-Derived Immunogens To Induce Clearance of Nontypeable Haemophilus influenzae from the Rat Middle Ear and Lungs as Well as from the Chinchilla Middle Ear and Nasopharynx." Infection and Immunity 71, no. 8 (August 2003): 4691–99. http://dx.doi.org/10.1128/iai.71.8.4691-4699.2003.

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ABSTRACT The rat middle ear and lung clearance model has been used to show that the nontypeable Haemophilus influenzae 26-kDa outer membrane protein OMP26 is highly efficacious as a mucosal immunogen, inducing significantly enhanced clearance in immunized rats upon direct challenge of these two anatomic sites. Similarly, the chinchilla model of middle ear and nasopharyngeal clearance has been used to show that two P5 fimbrin adhesin-derived immunogens, LB1 and lipoprotein D (LPD)-LB1(f)2,1,3, are highly efficacious as parenteral immunogens. Both induced significantly augmented clearance of nontypeable H. influenzae upon challenge of these sites. Here, these three nontypeable H. influenzae immunogens in addition to six bovine serum albumin and keyhole limpet hemocyanin conjugates of the synthetic peptide LB1(f) were assayed for relative efficacy in the reciprocal rodent model system. OMP26 was assayed in the chinchilla host by a parenteral immunization route, with clearance of the middle ear and nasopharynx used as outcome measures. Both LB1 and LPD-LB1(f)2,1,3 were assayed in the rat host with a mucosal immunization route and clearance of nontypeable H. influenzae from the lungs and middle ears as outcome measures. Both of the immunogens were found to induce a high-titered and specific immune responses in the heterologous host system. Moreover, each was found to be highly efficacious in the reciprocal host system, providing strong support for the continued development and inclusion of both OMP26 and P5 fimbrin-derived peptides as candidate vaccine antigens directed at otitis media caused by nontypeable H. influenzae.
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4

Manterola, Lorea, Caterina Guzmán-Verri, Esteban Chaves-Olarte, Elías Barquero-Calvo, María-Jesús de Miguel, Ignacio Moriyón, María-Jesús Grilló, Ignacio López-Goñi, and Edgardo Moreno. "BvrR/BvrS-Controlled Outer Membrane Proteins Omp3a and Omp3b Are Not Essential for Brucella abortus Virulence." Infection and Immunity 75, no. 10 (July 30, 2007): 4867–74. http://dx.doi.org/10.1128/iai.00439-07.

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ABSTRACT The Brucella abortus two-component regulatory system BvrR/BvrS controls the expression of outer membrane proteins (Omp) Omp3a (Omp25) and Omp3b (Omp22). Disruption of bvrS or bvrR generates avirulent mutants with altered cell permeability, higher sensitivity to microbicidal peptides, and complement. Consequently, the role of Omp3a and Omp3b in virulence was examined. Similar to bvrS or bvrR mutants, omp3a and omp3b mutants displayed increased attachment to cells, indicating surface alterations. However, they showed unaltered permeability; normal expression of Omp10, Omp16, Omp19, Omp2b, and Omp1; native hapten polysaccharide; and lipopolysaccharide and were resistant to complement and polymyxin B at ranges similar to those of the wild-type (WT) counterpart. Likewise, omp3a and omp3b mutants were able to replicate in murine macrophages and in HeLa cells, were resistant to the killing action of human neutrophils, and persisted in mice, like the WT strain. Murine macrophages infected with the omp3a mutant generated slightly higher levels of tumor necrosis factor alpha than the WT, whereas the bvrS mutant induced lower levels of this cytokine. Since the absence of Omp3a or Omp3b does not result in attenuation, it can be concluded that BvrR/BvrS influences additional Brucella properties involved in virulence. Our results are discussed in the light of previous works suggesting that disruption of omp3a generates attenuated Brucella strains, and we speculate on the role of group 3 Omps.
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5

Paquet, Jean-Yves, Maria A. Diaz, Stephanie Genevrois, Maggy Grayon, Jean-Michel Verger, Xavier De Bolle, Jeremy H. Lakey, Jean-Jacques Letesson, and Axel Cloeckaert. "Molecular, Antigenic, and Functional Analyses of Omp2b Porin Size Variants of Brucella spp." Journal of Bacteriology 183, no. 16 (August 15, 2001): 4839–47. http://dx.doi.org/10.1128/jb.183.16.4839-4847.2001.

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ABSTRACT Omp2a and Omp2b are highly homologous porins present in the outer membrane of the bacteria from the genus Brucella, a facultative intracellular pathogen. The genes coding for these proteins are closely linked in the Brucella genome and oriented in opposite directions. In this work, we present the cloning, purification, and characterization of four Omp2b size variants found in various Brucella species, and we compare their antigenic and functional properties to the Omp2a and Omp2b porins ofBrucella melitensis reference strain 16M. The variation of the Omp2a and Omp2b porin sequences among the various strains of the genus Brucella seems to result mostly from multiple gene conversions between the two highly homologous genes. As shown in this study, this phenomenon has led to the creation of natural Omp2a and Omp2b chimeric proteins in Omp2b porin size variants. The comparison by liposome swelling assay of the porins sugar permeability suggested a possible functional differences between Omp2a and Omp2b, with Omp2a showing a more efficient pore in sugar diffusion. The sequence variability in the Omp2b size variants was located in the predicted external loops of the porin. Several epitopes recognized by anti-Omp2b monoclonal antibodies were mapped by comparison of the Omp2b size variants antigenicity, and two of them were located in the most exposed surface loops. However, since variations are mostly driven by simple exchanges of conserved motifs between the two genes (except for an Omp2b version from an atypical strain of Brucella suisbiovar 3), the porin variability does not result in major antigenic variability of the Brucella surface that could help the bacteria during the reinfection of a host. Porin variation inBrucella seems to result mainly in porin conductivity modifications.
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6

Bramanti, T. E., and S. C. Holt. "Hemin uptake in Porphyromonas gingivalis: Omp26 is a hemin-binding surface protein." Journal of Bacteriology 175, no. 22 (1993): 7413–20. http://dx.doi.org/10.1128/jb.175.22.7413-7420.1993.

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7

Farquharson, Kara Louise, Niaya Jackson, Susan Shi Cheng, Ravinder Kaur, and Lea Vacca Michel. "Elucidating the Protein‐Protein Interactions between Nontypeable Haemophilus Influenzae Outer Membrane Proteins Omp26 and Protein D." FASEB Journal 34, S1 (April 2020): 1. http://dx.doi.org/10.1096/fasebj.2020.34.s1.02607.

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8

Eisenberg, Tobias, Hans-Peter Hamann, Ute Kaim, Karen Schlez, Helga Seeger, Nicole Schauerte, Falk Melzer, et al. "Isolation of Potentially Novel Brucella spp. from Frogs." Applied and Environmental Microbiology 78, no. 10 (March 9, 2012): 3753–55. http://dx.doi.org/10.1128/aem.07509-11.

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ABSTRACTBacterial isolates from frogs were phenotypically identified asOchrobactrum anthropi, but 16S rRNA sequencing showed up to 100% identity withBrucella inopinata. Further analysis ofrecA,omp2a,omp2b,bcsp31, and IS711and multilocus sequence analysis (MLSA) verified a close relationship withBrucella, suggesting the isolates may actually represent novel members of this growing genus of zoonotic pathogens.
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9

Caro-Hernández, Paola, Luis Fernández-Lago, María-Jesús de Miguel, Ana I. Martín-Martín, Axel Cloeckaert, María-Jesús Grilló, and Nieves Vizcaíno. "Role of the Omp25/Omp31 Family in Outer Membrane Properties and Virulence of Brucella ovis." Infection and Immunity 75, no. 8 (June 11, 2007): 4050–61. http://dx.doi.org/10.1128/iai.00486-07.

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ABSTRACT The genes coding for the five outer membrane proteins (OMPs) of the Omp25/Omp31 family expected to be located in the outer membrane (OM) of rough virulent Brucella ovis PA were inactivated to evaluate their role in virulence and OM properties. The OM properties of the mutant strains and of the mutants complemented with the corresponding wild-type genes were analyzed, in comparison with the parental strain and rough B. abortus RB51, in several tests: (i) binding of anti-Omp25 and anti-Omp31 monoclonal antibodies, (ii) autoagglutination of bacterial suspensions, and (iii) assessment of susceptibility to polymyxin B, sodium deoxycholate, hydrogen peroxide, and nonimmune ram serum. A tight balance of the members of the Omp25/Omp31 family was seen to be essential for the stability of the B. ovis OM, and important differences between the OMs of B. ovis PA and B. abortus RB51 rough strains were observed. Regarding virulence, the absence of Omp25d and Omp22 from the OM of B. ovis PA led to a drastic reduction in spleen colonization in mice. While the greater susceptibility of the Δomp22 mutant to nonimmune serum and its difficulty in surviving in the stationary phase might be on the basis of its dramatic attenuation, no defects in the OM able to explain the attenuation of the Δomp25d mutant were found, especially considering that the fully virulent Δomp25c mutant displayed more important OM defects. Accordingly, Omp25d, and perhaps Omp22, could be directly involved in the penetration and/or survival of B. ovis inside host cells. This aspect, together with the role of Omp25d and Omp22 in the virulence both of B. ovis in rams and of other Brucella species, should be thoroughly evaluated in future studies.
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10

Khan, M. Nadeem, Ravinder Kaur, and Michael E. Pichichero. "Bactericidal antibody response against P6, protein D, and OMP26 of nontypeableHaemophilus influenzaeafter acute otitis media in otitis-prone children." FEMS Immunology & Medical Microbiology 65, no. 3 (August 2012): 439–47. http://dx.doi.org/10.1111/j.1574-695x.2012.00967.x.

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11

Mobasheri, H., T. A. Ficht, H. Marquis, E. J. A. Lea, and J. H. Lakey. "Brucella Omp2a and Omp2b porins: single channel measurements and topology prediction." FEMS Microbiology Letters 155, no. 1 (January 17, 2006): 23–30. http://dx.doi.org/10.1111/j.1574-6968.1997.tb12681.x.

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12

Salhi, Imed, Rose-Anne Boigegrain, Jan Machold, Christoph Weise, Axel Cloeckaert, and Bruno Rouot. "Characterization of New Members of the Group 3 Outer Membrane Protein Family of Brucella spp." Infection and Immunity 71, no. 8 (August 2003): 4326–32. http://dx.doi.org/10.1128/iai.71.8.4326-4332.2003.

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ABSTRACT Impairment of the omp25 gene in Brucella spp. leads to attenuated strains and confers protection to the host. Omp25 and Omp31, whose functions remain unknown, were the first characterized members of group 3 outer membrane proteins (Omps) (25 to 34 kDa). Recently, genomic and proteomic approaches identified five new putative members of this family, some of which are produced in B. melitensis or B. abortus. In the present study, using protein microsequencing, we identified new members of group 3 Omps proteins produced in B. suis. Since several monoclonal antibodies (MAbs) against Omp25 cross-reacted with other members of group 3 Omps, we also performed Western immunoblotting to compare wild-type B. suis with mutants systematically having B. suis omp25-related genes knocked out. We demonstrate the production of three paralogs of Omp31 and/or Omp25 in B. suis, and the existence of a common site of signal peptide cleavage (AXAAD), which is very similar to that present in the five homologous Omps of Bartonella quintana. The seven group 3 Omps were classified in four-subgroups on the basis of percentage amino acid sequence identities: Omp25 alone, the Omp25b-Omp25c-Omp25d cluster, the Omp31/31b subgroup, and the less related Omp22 protein (also called Omp3b). Together with previous data, our results demonstrate that all new members of group 3 Omps are produced in B. suis or in other Brucella species and we propose a nomenclature that integrates all of these proteins to facilitate the understanding of future Brucella interspecies study results.
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13

Riedmann, Eva M., Werner Lubitz, John McGrath, Jennelle M. Kyd, and Allan W. Cripps. "Effectiveness of engineering the nontypeableHaemophilus influenzaeantigen Omp26 as an S-layer fusion in bacterial ghosts as a mucosal vaccine delivery." Human Vaccines 7, sup1 (January 2011): 99–107. http://dx.doi.org/10.4161/hv.7.0.14569.

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14

Lü, Lin, Han-qing Zeng, Pi-long Wang, Wei Shen, Ting-xiu Xiang, and Zhe-chuan Mei. "Oral Immunization with Recombinant Mycobacterium smegmatis Expressing the Outer Membrane Protein 26-Kilodalton Antigen Confers Prophylactic Protection against Helicobacter pylori Infection." Clinical and Vaccine Immunology 18, no. 11 (September 7, 2011): 1957–61. http://dx.doi.org/10.1128/cvi.05306-11.

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ABSTRACTHelicobacter pyloriinfection is prevalent worldwide and results in chronic gastritis, which may lead to gastric mucosa-associated lymphoid tissue lymphoma and gastric cancer. We have previously reported that oral immunization with recombinantMycobacterium smegmatisexpressing theH. pyloriouter membrane protein 26-kilodalton (Omp26) antigen affords therapeutic protection againstH. pyloriinfection in mice. In the present study, we investigated the prophylactic effects of this vaccine candidate onH. pylorichallenge in mice. We found that oral immunization with recombinantMycobacteriumOmp26 significantly reducedH. pyloricolonization in the stomach compared to inoculation with wild-typeM. smegmatisin control mice. Six of the recombinantMycobacterium-immunized mice (60%) were completely protected fromH. pyloriinfection. The severity ofH. pylori-associated chronic gastritis assessed histologically was significantly milder in mice vaccinated with recombinantMycobacteriumthan in control animals. Mice immunized with recombinantMycobacteriumshowed enhanced antigen-specific lymphocyte proliferation and antibody responses. Moreover, immunization with recombinantMycobacteriumresulted in an increased expression of interleukin-2 and gamma interferon in the stomach and spleen, as determined by reverse transcription-PCR analysis. Our results collectively suggest that vaccination with recombinantMycobacteriumOmp26 confers prophylactic protection againstH. pyloriinfection. The inhibition ofH. pyloricolonization is associated with the induction of antigen-specific humoral and cell-mediated immune responses.
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15

Pichichero, Michael E., Ravinder Kaur, Janet R. Casey, Albert Sabirov, M. Nadeem Khan, and Anthony Almudevar. "Antibody response to Haemophilus influenzae outer membrane protein D, P6, and OMP26 after nasopharyngeal colonization and acute otitis media in children." Vaccine 28, no. 44 (October 2010): 7184–92. http://dx.doi.org/10.1016/j.vaccine.2010.08.063.

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16

El-Adhami, Wafa, Jennelle M. Kyd, David A. Bastin, and Allan W. Cripps. "Characterization of the Gene Encoding a 26-Kilodalton Protein (OMP26) from Nontypeable Haemophilus influenzae and Immune Responses to the Recombinant Protein." Infection and Immunity 67, no. 4 (1999): 1935–42. http://dx.doi.org/10.1128/.67.4.1935-1942.1999.

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17

Scholz, Holger C., Karsten Nöckler, Cornelia Göllner, Peter Bahn, Gilles Vergnaud, Herbert Tomaso, Sascha Al Dahouk, et al. "Brucella inopinata sp. nov., isolated from a breast implant infection." International Journal of Systematic and Evolutionary Microbiology 60, no. 4 (April 1, 2010): 801–8. http://dx.doi.org/10.1099/ijs.0.011148-0.

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A Gram-negative, non-motile, non-spore-forming coccoid bacterium (strain BO1T) was isolated recently from a breast implant infection of a 71-year-old female patient with clinical signs of brucellosis. Affiliation of strain BO1T to the genus Brucella was confirmed by means of polyamine pattern, polar lipid profile, fatty acid profile, quinone system, DNA–DNA hybridization studies and by insertion sequence 711 (IS711)-specific PCR. Strain BO1T harboured four to five copies of the Brucella-specific insertion element IS711, displaying a unique banding pattern, and exhibited a unique 16S rRNA gene sequence and also grouped separately in multilocus sequence typing analysis. Strain BO1T reacted with Brucella M-monospecific antiserum. Incomplete lysis was detected with bacteriophages Tb (Tbilisi), F1 and F25. Biochemical profiling revealed a high degree of enzymic activity and metabolic capabilities. In multilocus VNTR (variable-number tandem-repeat) analysis, strain BO1T showed a very distinctive profile and clustered with the other ‘exotic’ Brucella strains, including strains isolated from marine mammals, and Brucella microti, Brucella suis biovar 5 and Brucella neotomae. Comparative omp2a and omp2b gene sequence analysis revealed the most divergent omp2 sequences identified to date for a Brucella strain. The recA gene sequence of strain BO1T differed in seven nucleotides from the Brucella recA consensus sequence. Using the Brucella species-specific multiplex PCR assay, strain BO1T displayed a unique banding pattern not observed in other Brucella species. From the phenotypic and molecular analysis it became evident that strain BO1T was clearly different from all other Brucella species, and therefore represents a novel species within the genus Brucella. Because of its unexpected isolation, the name Brucella inopinata with the type strain BO1T (=BCCN 09-01T=CPAM 6436T) is proposed.
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18

Kim, Nayoung, David L. Weeks, Jai Moo Shin, David R. Scott, Mary K. Young, and George Sachs. "Proteins Released by Helicobacter pylori In Vitro." Journal of Bacteriology 184, no. 22 (November 15, 2002): 6155–62. http://dx.doi.org/10.1128/jb.184.22.6155-6162.2002.

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ABSTRACT Secretion of proteins by Helicobacter pylori may contribute to gastric inflammation and epithelial damage. An in vitro analysis was designed to identify proteins released by mechanisms other than nonspecific lysis. The radioactivity of proteins in the supernatant was compared with that of the intact organism by two-dimensional gel phosphorimaging following a 4-h pulse-chase. The ratio of the amount of UreB, a known cytoplasmic protein, in the supernatant to that in the pellet was found to be 0.25, and this was taken as an index of lysis during the experiments (n = 6). Ratios greater than that of UreB were used to distinguish proteins that were selectively released into the medium. Thus, proteins enriched more than 10-fold in the supernatant compared to UreB were identified by mass spectrometry. Sixteen such proteins were present in the supernatant: VacA; a conserved secreted protein (HP1286); putative peptidyl cis-trans isomerase (HP0175); six proteins encoded by HP0305, HP0231, HP0973, HP0721, HP0129, and HP0902; thioredoxin (HP1458); single-stranded-DNA-binding 12RNP2 precursor (HP0827); histone-like DNA-binding protein HU (HP0835); ribosomal protein L11 (HP1202); a putative outer membrane protein (HP1564); and outer membrane proteins Omp21 (HP0913) and Omp20 (HP0912). All except HP0902, thioredoxin, HP0827, HP0835, and HP1202 had a signal peptide. When nalidixic acid, a DNA synthesis inhibitor, was added to inhibit cell division but not protein synthesis, to decrease possible contamination due to outer membrane shedding, two outer membrane proteins (Omp21 and Omp20) disappeared from the supernatant, and the amount of VacA also decreased. Thus, 13 proteins were still enriched greater than 10-fold in the medium after nalidixic acid treatment, suggesting these were released specifically, possibly by secretion. These proteins may be implicated in H. pylori-induced effects on the gastric epithelium.
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Avila-Calderón, Eric Daniel, Ahidé Lopez-Merino, Neeta Jain, Humberto Peralta, Edgar Oliver López-Villegas, Nammalwar Sriranganathan, Stephen M. Boyle, Sharon Witonsky, and Araceli Contreras-Rodríguez. "Characterization of Outer Membrane Vesicles fromBrucella melitensisand Protection Induced in Mice." Clinical and Developmental Immunology 2012 (2012): 1–13. http://dx.doi.org/10.1155/2012/352493.

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The outer membrane vesicles (OMVs) from smoothB. melitensis16 M and a derived rough mutant, VTRM1 strain, were purified and characterized with respect to protein content and induction of immune responses in mice. Proteomic analysis showed 29 proteins present in OMVs fromB. melitensis16 M; some of them are well-knownBrucellaimmunogens such as SOD, GroES, Omp31, Omp25, Omp19, bp26, and Omp16. OMVs from a rough VTRM1 induced significantly higher expression of IL-12, TNFα, and IFNγ genes in bone marrow dendritic cells than OMVs from smooth strain 16 M. Relative to saline control group, mice immunized intramuscularly with rough and smooth OMVs were protected from challenge with virulent strainB. melitensis16 M just as well as the group immunized with live strainB. melitensisRev1 (P<0.005). Additionally, the levels of serum IgG2a increased in mice vaccinated with OMVs from rough strain VTRM1 consistent with the induction of cell-mediated immunity.
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Pasquevich, Karina A., Silvia M. Estein, Clara García Samartino, Astrid Zwerdling, Lorena M. Coria, Paula Barrionuevo, Carlos A. Fossati, Guillermo H. Giambartolomei, and Juliana Cassataro. "Immunization with Recombinant Brucella Species Outer Membrane Protein Omp16 or Omp19 in Adjuvant Induces Specific CD4+ and CD8+ T Cells as Well as Systemic and Oral Protection against Brucella abortus Infection." Infection and Immunity 77, no. 1 (November 3, 2008): 436–45. http://dx.doi.org/10.1128/iai.01151-08.

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ABSTRACT Available vaccines against Brucella spp. are live attenuated Brucella strains. In order to engineer a better vaccine to be used in animals and humans, our laboratory aims to develop an innocuous subunit vaccine. Particularly, we are interested in the outer membrane proteins (OMPs) of B. abortus: Omp16 and Omp19. In this study, we assessed the use of these proteins as vaccines against Brucella in BALB/c mice. Immunization with lipidated Omp16 (L-Omp16) or L-Omp19 in incomplete Freund's adjuvant (IFA) conferred significant protection against B. abortus infection. Vaccination with unlipidated Omp16 (U-Omp16) or U-Omp19 in IFA induced a higher degree of protection than the respective lipidated versions. Moreover, the level of protection induced after U-Omp16 or U-Omp19 immunization in IFA was similar to that elicited by live B. abortus S19 immunization. Flow cytometric analysis showed that immunization with U-Omp16 or U-Omp19 induced antigen-specific CD4+ as well as CD8+ T cells producing gamma interferon. In vivo depletion of CD4+ or CD8+ T cells in mice immunized with U-Omp16 or U-Omp19 plus IFA resulted in a loss of the elicited protection, indicating that both cell types are mediating immune protection. U-Omp16 or U-Omp19 vaccination induced a T helper 1 response, systemic protection in aluminum hydroxide formulation, and oral protection with cholera toxin adjuvant against B. abortus infection. Both immunization routes exhibited a similar degree of protection to attenuated Brucella vaccines (S19 and RB51, respectively). Overall these results indicate that U-Omp16 or U-Omp19 would be a useful candidate for a subunit vaccine against human and animal brucellosis.
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Sumie, Akihiro, Tetsu Yamashiro, Kazutoshi Nakashima, Masaru Nasu, Makoto Watanabe, and Akira Nishizono. "Comparison of Genomic Structures and Antigenic Reactivities of Orthologous 29-Kilodalton Outer Membrane Proteins ofHelicobacter pylori." Infection and Immunity 69, no. 11 (November 1, 2001): 6846–52. http://dx.doi.org/10.1128/iai.69.11.6846-6852.2001.

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ABSTRACT We purified a 29-kDa Helicobacter pylori outer membrane protein (Omp29 protein) and cloned the gene encoding the protein from H. pylori strain ATCC 43504. The Omp29 gene corresponded to the reported JHP73 and the HP78–79 genes of H. pylori strains. A corresponding nucleotide fragment was detected in all 150 tested H. pylori clinical isolates by PCR or Southern blotting. The amplified Omp29-corresponding fragments were categorized into a ca. 770-bp-long group and a larger-fragment group. Sequence analysis indicated that the larger fragments were likely synthesized from the 770-bp fragments by insertion of an irrelevant fragment via 17-bp-long repeat sequences. Immunoblot analysis implies that the ca. 770-bp fragment is responsible for the protein homologous to Omp29, whereas the larger fragments are not responsible for those proteins or encoding antigenically distinct proteins. We postulate that the H. pylori outer membrane protein Omp29 can alter its antigenicity through gene modifications mediated by nucleotide transfer.
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Luo, Deyan, Bing Ni, Peng Li, Wei Shi, Songle Zhang, Yue Han, Liwei Mao, Yangdong He, Yuzhang Wu, and Xiliang Wang. "Protective Immunity Elicited by a Divalent DNA Vaccine Encoding Both the L7/L12 and Omp16 Genes of Brucella abortus in BALB/c Mice." Infection and Immunity 74, no. 5 (May 2006): 2734–41. http://dx.doi.org/10.1128/iai.74.5.2734-2741.2006.

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ABSTRACT This study was designed to evaluate the immunogenicity and the protective efficacy of a divalent fusion DNA vaccine encoding both the Brucella abortus L7/L12 protein (ribosomal protein) and Omp16 protein (outer membrane lipoprotein), designated pcDNA3.1-L7/L12-Omp16. Intramuscular injection of this divalent DNA vaccine into BALB/c mice elicited markedly both humoral and cellular immune responses. The specific antibodies exhibited a dominance of immunoglobulin G2a (IgG2a) over IgG1. In addition, the dual-gene DNA vaccine elicited a strong T-cell proliferative response and induced a large amount of gamma interferon-producing T cells upon restimulation in vitro with recombinant fusion protein L7/L12-Omp16, suggesting the induction of a typical T-helper-1-dominated immune response in vivo. This divalent DNA vaccine could also induce a significant level of protection against challenge with the virulent strain B. abortus 544 in BALB/c mice. Furthermore, the protection level induced by the divalent DNA vaccine was significantly higher than that induced by the univalent DNA vaccines pcDNA3.1-L7/L12 or pcDNA3.1-Omp16. Taken together, the results of this study verify for the first time that the Omp16 gene can be a candidate target for a DNA vaccine against brucellosis. Additionally, a divalent genetic vaccine based on the L7/L12 and Omp16 genes can elicit a stronger cellular immune response and better immunoprotection than the relevant univalent vaccines can.
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Rezaei, Marzieh, Mohammad Rabbani Khorasgani, Sayyed Hamid Zarkesh Esfahani, Rahman Emamzadeh, and Hamid Abtahi. "Production of Brucella melitensis Omp16 protein fused to the human interleukin 2 in Lactococcus lactis MG1363 toward developing a Lactococcus-based vaccine against brucellosis." Canadian Journal of Microbiology 66, no. 1 (January 2020): 39–45. http://dx.doi.org/10.1139/cjm-2019-0261.

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The use of the food-grade bacterium Lactococcus lactis as a new cell factory is a promising alternative expression system for producing a desired protein. The Omp16-IL2 fusion protein antigen was cloned, expressed, and purified in this study. The Omp16-IL2 fusion gene was designed and cloned in pGH plasmid with appropriate restriction sites and subcloned in pAMJ2008 expression vector digested with the same enzymes. The purified recombinant constructed pAMJ-rOmp-IL2 was introduced into L. lactis subsp. cremoris MG1363 by electrotransformation. Finally, the expression and purification of Omp16-IL2 fusion protein was investigated. This study reports the construction of a recombinant L. lactis expressing the Omp16-IL2 fusion protein as an oral Lactococcus-based vaccine, as compared with commonly used live attenuated vaccines, for future studies against brucellosis.
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Gupta, Sonal, Surender Mohan, Vikas Kumar Somani, Somya Aggarwal, and Rakesh Bhatnagar. "Simultaneous Immunization with Omp25 and L7/L12 Provides Protection against Brucellosis in Mice." Pathogens 9, no. 2 (February 24, 2020): 152. http://dx.doi.org/10.3390/pathogens9020152.

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Currently used Brucella vaccines, Brucella abortus strain 19 and RB51, comprises of live attenuated Brucella strains and prevent infection in animals. However, these vaccines pose potential risks to recipient animals such as attenuation reversal and virulence in susceptible hosts on administration. In this context, recombinant subunit vaccines emerge as a safe and competent alternative in combating the disease. In this study, we formulated a divalent recombinant vaccine consisting of Omp25 and L7/L12 of B. abortus and evaluated vaccine potential individually as well as in combination. Sera obtained from divalent vaccine (Omp25+L7/L12) immunized mice group exhibited enhanced IgG titers against both components and indicated specificity upon immunoblotting reiterating its authenticity. Further, the IgG1/IgG2a ratio obtained against each antigen predicted a predominant Th2 immune response in the Omp25+L7/L12 immunized mice group. Upon infection with virulent B. abortus 544, Omp25+L7/L12 infected mice exhibited superior Log10 protection compared to individual vaccines. Consequently, this study recommends that simultaneous immunization of Omp25 and L7/L12 as a divalent vaccine complements and triggers a Th2 mediated immune response in mice competent of providing protection against brucellosis.
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Baldermann, C., A. Lupas, J. Lubieniecki, and H. Engelhardt. "The Regulated Outer Membrane Protein Omp21 from Comamonas acidovorans Is Identified as a Member of a New Family of Eight-Stranded β-Sheet Proteins by Its Sequence and Properties." Journal of Bacteriology 180, no. 15 (August 1, 1998): 3741–49. http://dx.doi.org/10.1128/jb.180.15.3741-3749.1998.

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ABSTRACT Omp21, a minor outer membrane protein of the soil bacteriumComamonas acidovorans, was purified from a spontaneous mutant lacking a surface layer and long-chain lipopolysaccharide. Omp21 synthesis is enhanced by oxygen depletion, and the protein has a variable electrophoretic mobility in sodium dodecyl sulfate-polyacrylamide gel electrophoresis due to its heat-modifiable behavior. The structural gene omp21 encodes a precursor of 204 amino acids with a putative signal peptide of 21 amino acids. Mature Omp21 is a typical outer membrane protein with a high content of β structure as determined by infrared spectroscopy. Sequence comparisons show that it belongs to a new outer membrane protein family, characterized by eight amphipathic β strands, which includes virulence proteins, such as the neisserial opacity proteins,Salmonella typhimurium Rck, and Yersinia enterocolitica Ail, as well as the major outer membrane proteins OmpA from Escherichia coli and OprF fromPseudomonas aeruginosa.
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Jubier-Maurin, Véronique, Rose-Anne Boigegrain, Axel Cloeckaert, Antoine Gross, Maria-Teresa Alvarez-Martinez, Annie Terraza, Janny Liautard, et al. "Major Outer Membrane Protein Omp25 of Brucella suis Is Involved in Inhibition of Tumor Necrosis Factor Alpha Production during Infection of Human Macrophages." Infection and Immunity 69, no. 8 (August 1, 2001): 4823–30. http://dx.doi.org/10.1128/iai.69.8.4823-4830.2001.

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ABSTRACT Brucella spp. can establish themselves and cause disease in humans and animals. The mechanisms by whichBrucella spp. evade the antibacterial defenses of their host, however, remain largely unknown. We have previously reported that live brucellae failed to induce tumor necrosis factor alpha (TNF-α) production upon human macrophage infection. This inhibition is associated with a nonidentified protein that is released into culture medium. Outer membrane proteins (OMPs) of gram-negative bacteria have been shown to modulate macrophage functions, including cytokine production. Thus, we have analyzed the effects of two major OMPs (Omp25 and Omp31) of Brucella suis 1330 (wild-type [WT] B. suis) on TNF-α production. For this purpose, omp25and omp31 null mutants of B. suis(Δomp25 B. suis and Δomp31 B. suis, respectively) were constructed and analyzed for the ability to activate human macrophages to secrete TNF-α. We showed that, in contrast to WTB. suis or Δomp31 B. suis, Δomp25 B. suis induced TNF-α production when phagocytosed by human macrophages. The complementation of Δomp25 B. suis with WT omp25 (Δomp25-omp25 B. suis mutant) significantly reversed this effect: Δomp25-omp25 B. suis-infected macrophages secreted significantly less TNF-α than did macrophages infected with the Δomp25 B. suismutant. Furthermore, pretreatment of WT B. suis with an anti-Omp25 monoclonal antibody directed against an epitope exposed at the surface of the bacteria resulted in substancial TNF-α production during macrophage infection. These observations demonstrated that Omp25 of B. suis is involved in the negative regulation of TNF-α production upon infection of human macrophages.
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Mygind, Per, Gunna Christiansen, Kenneth Persson, and Svend Birkelund. "Analysis of the Humoral Immune Response toChlamydia Outer Membrane Protein 2." Clinical Diagnostic Laboratory Immunology 5, no. 3 (May 1, 1998): 313–18. http://dx.doi.org/10.1128/cdli.5.3.313-318.1998.

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ABSTRACT The humoral immune response to Chlamydia outer membrane protein 2 (Omp2) was studied. Omp2 is a highly genus-conserved structural protein of all Chlamydia species, containing a variable N-terminal fragment. To analyze where the immunogenic parts were localized, seven highly purified truncated fusion proteins constituting different regions of the protein were produced (Chlamydia pneumoniae-Omp2aa23-aa93,Chlamydia psittaci-Omp2aa23-aa94, andChlamydia trachomatis-Omp2aa23-aa84, aa87-aa547, aa23-aa182, aa167-aa434, aa420-aa547). By an enzyme-linked immunosorbent assay with serologically defined patient sera, Omp2 was found to be a major immunogen of both C. pneumoniae andC. trachomatis infections (P ≪ 0.0001). The humoral immune responses were not confined to any particular region of the Omp2 protein, and no species-specific anti-Omp2 immunoglobulins were detected.
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Ratnasari, Ratih, Didik Handijatno, Suwarno, and Fedik Abdul Rantam. "Determinan Antigen Gen omp2a Brucella abortus Isolat Lokal." Acta VETERINARIA Indonesiana 2, no. 1 (December 15, 2014): 17–25. http://dx.doi.org/10.29244/avi.2.1.17-25.

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Penyakit Brucellosis pada sapi disebabkan oleh Brucella abortus dan dikenal sebagai penyakitreproduksi menular pada ternak. Brucellosis merupakan penyakit zoonosis karena dapat menularpada manusia. Penelitian ini bertujuan untuk mengetahui determinan antigen yang terdapat pada genomp2a B. abortus isolat lokal yang telah diblasting ke asam amino (protein). Sampel bakteri berasaldari sapi penderita Brucellosis asal Sulawesi Selatan dan Nusa Tenggara Timur. Gen omp2a diamplifikasimelalui tehnik Polymerase Chain Reaction (PCR) dengan menggunakan primer 2ab5F dan 2a900R.Produk PCR disekuensing untuk mendapatkan sekuen nukleotida gen omp2a B. abortus isolat lokal.Sekuen nukleotida ini dianalisis tingkat homologinya terhadap isolat asal mancanegara yang diaksesdari GenBank dengan menggunakan BLAST. Sekuen nukleotida gen omp2a diblasting ke asam aminokemudian dengan metode Kolaskar dan Tongaonkar antigenicity dapat diperoleh determinan antigenpada antigen protein membran luar (OMP) B. abortus isolat lokal. Hasil menunjukkan bahwa tingkathomologi antara sekuen gen omp2a B. abortus isolat lokal dengan isolat asal mancanegara mempunyaitingkat homologi yang tinggi (99% - 100%). Hasil prediksi determinan antigen didapatkan enamdeterminan antigen pada antigen OMP B. abortus isolat lokal.
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Ilgekbaeva,, G. D., E. Sh Makhashov, G. Tulepova, D. Yessimkhankyzy, and S. T. Sadiev. "EXPRESSION OF THE SURFACE ANTIGEN BRUCELLA ABORTUS OMR16 IN NICOTIANA BENTHAMIANA PLANT." REPORTS 5, no. 333 (October 15, 2020): 81–85. http://dx.doi.org/10.32014/2020.2518-1483.122.

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Brucellosis is one of the most contagious and infectious diseases with high incidence rates of cattle and humans in Kazakhstan. Using modern biotechnology techniques to develop vaccines that are reliable and affordable for farmers is an alternative solution to the problem. Plant viruses are often used as a vector for obtaining the expression of antigens of the pathogen. The grape virus A (BAB) is widely used among plant viruses. Brucella membrane proteins are the main objects of this research for futher development of vaccines or diagnostic texts against brucellosis, Membrane proteins (OMPs) are cell specific surface antigens that are immunogenic. OMPs are ideal candidates for the production of recombinant brucellosis vaccines. The object of the study was the outer membrane protein (Omp16), which plays an important role in the suppression of TNF-α production in macrophages. In this study, molecular cloning and analysis of the expression of the Omp16 gene, which was used to express the recombinant protein in plants, was carried out. We selected brucella from the vaccine strain of Brucella abortus 19, and the plant Nicotiana benthamiana, as the subjects for our research, since they widely used for the production of recombinant proteins, and they both appropriate for molecular genetic research. A viral vector was constructed to express the brucellosis antigen Omp16 in Nicotiana benthamiana plants. Nineteen explants were used for the regeneration of transgenic plants. As a result of this studies, the introduced gene of Omp16 was under the subgenomic promoter control of the ORF4 and was successfully expressed while maintaining the efficiency of expression in transgenic plants. The efficiency of viral vectors was evaluated at the level of transcription during expression of the protein Omp16 with viral proteins. The entire leaf blade was infiltrated; the density of Agrobacteria was 0.7. We were able to obtained transgenic plants Nicotiana benthamiana carrying the gene of capsid protein BAB, and the expression of the membrane antigen Omp16 in the viral vector was achieved by replacing the ORF4 with the Omp16 gene. The development of transgenic plants was carried out using agrobacterial transformation.
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Mygind, Per, Gunna Christiansen, and Svend Birkelund. "Topological Analysis of Chlamydia trachomatis L2 Outer Membrane Protein 2." Journal of Bacteriology 180, no. 21 (November 1, 1998): 5784–87. http://dx.doi.org/10.1128/jb.180.21.5784-5787.1998.

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ABSTRACT Using monospecific polyclonal antisera to different parts ofChlamydia trachomatis L2 outer membrane protein 2 (Omp2), we show that the protein is localized at the inner surface of the outer membrane. Omp2 becomes immunoaccessible when Chlamydiaelementary bodies are treated with dithiothreitol, and protease digestions indicate that Omp2 has a possible two-domain structure.
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31

Kim, Won-Seok, Jeong Sun-Hyung, Ro-Dong Park, Kil-Yong Kim, and Hari B. Krishnan. "Sinorhizobium fredii USDA257 Releases a 22-kDa Outer Membrane Protein (Omp22) to the Extracellular Milieu When Grown in Calcium-Limiting Conditions." Molecular Plant-Microbe Interactions® 18, no. 8 (August 2005): 808–18. http://dx.doi.org/10.1094/mpmi-18-0808.

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Calcium, which regulates a wide variety of cellular functions, plays an important role in Rhizobium-legume interactions. We investigated the effect of calcium on surface appendages of Sinorhizobium fredii USDA257. Cold-field emission scanning electron microscopy observation of USDA257 grown in calcium-limiting conditions revealed cells with unusual shape and size. Transmission electron microscopy observation revealed intact flagella were present only when USDA257 cells were grown in calcium-sufficient conditions. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis of flagellar preparations from USDA257 cells grown in calcium-limiting conditions showed the presence of a 22-kDa protein that was absent from cells grown in calcium-sufficient conditions. We have cloned and determined the nucleotide sequence of the gene encoding the 22- kDa protein. After successful expression in Escherichia coli, polyclonal antibodies were raised against the recombinant 22-kDa protein (Omp22). Subcellular fractionation analysis demonstrated that Omp22 was predominantly present in the extracellular fraction. Western blot analysis revealed the presence of immunologically related proteins from diverse rhizobia. Immunocytochemical localization of thin sections of USDA257 cells showed specific labeling of protein A-gold particles on protein inclusions found proximal to the cells. Accumulation of Omp22 was greatly reduced when USDA257 cells were grown in the presence of increasing calcium. Northern blot analysis indicated that calcium was the only divalent cation among those tested that down-regulated omp22 expression. An omp22 mutant was able to grow in calcium-limiting conditions at a rate similar to that of wild-type USDA257. Significantly more nodules were initiated by the omp22 mutant than by the wild-type on soybean cultivar Peking grown in calciumlimiting conditions.
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32

Portig, I., J. C. Goodall, R. L. Bailey, and J. S. H. Gaston. "Characterization of the Humoral Immune Response to Chlamydia Outer Membrane Protein 2 in Chlamydial Infection." Clinical Diagnostic Laboratory Immunology 10, no. 1 (January 2003): 103–7. http://dx.doi.org/10.1128/cdli.10.1.103-107.2003.

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ABSTRACT Detection of antibodies to an outer membrane protein 2 (OMP2) by enzyme-linked immunosorbent assay (ELISA) by using either the Chlamydia trachomatis- or the Chlamydia pneumoniae-specific protein was investigated. OMP2 is an immunodominant antigen giving rise to antibody responses in humans infected with different C. trachomatis serovars (A to C and D to K) or with C. pneumoniae, which could be detected by OMP2 ELISA. OMP2 ELISA is not species specific, but antibody titers were usually higher on the homologous protein. The sensitivity of this assay was high but varied according to the “gold standard” applied. Levels of antibody to C. pneumoniae OMP2 as detected by ELISA seem to return to background or near-background values within a shorter period of time compared to antibodies to C. pneumoniae detected by microimmunofluorescence (MIF), making it more likely that positive results in ELISA reflect recent infection. Thus, OMP2 ELISA has distinct advantages over MIF and commercially available ELISAs and might be a useful tool for the serodiagnosis of chlamydial infection.
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Chervyakova, Olga, Elmira Tailakova, Nurlan Kozhabergenov, Sandugash Sadikaliyeva, Kulyaisan Sultankulova, Kunsulu Zakarya, Rinat A. Maksyutov, Vitaliy Strochkov, and Nurlan Sandybayev. "Engineering of Recombinant Sheep Pox Viruses Expressing Foreign Antigens." Microorganisms 9, no. 5 (May 7, 2021): 1005. http://dx.doi.org/10.3390/microorganisms9051005.

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Capripoxviruses with a host range limited to ruminants have the great potential to be used as vaccine vectors. The aim of this work was to evaluate attenuated sheep pox virus (SPPV) vaccine strain NISKHI as a vector expressing several genes. Open reading frames SPPV020 (ribonucleotide kinase) and SPPV066 (thymidine kinase) were selected as sites for the insertion of foreign genes. Two integration plasmids with expression cassette were designed and constructed. Recombinant SPPVs expressing an enhanced green fluorescent protein (EGFP) (rSPPV(RRΔ)EGFP and rSPPV(TKΔ)EGFP), Foot-and-mouth disease virus capsid protein (VP1), and Brucella spp. outer membrane protein 25 (OMP25) (rSPPV(RRΔ)VP1A-(TKΔ)OMP25) were generated under the transient dominant selection method. The insertion of foreign genes into the SPPV020 and SPPV066 open reading frames did not influence the replication of the recombinant viruses in the cells. Successful foreign gene expression in vitro was assessed by luminescent microscopy (EGFP) and Western blot (VP1 and OMP25). Our results have shown that foreign genes were expressed by rSPPV both in permissive (lamb testicles) and non-permissive (bovine kidney, saiga kidney, porcine kidney) cells. Mice immunized with rSPPV(RRΔ)VP1A-(TKΔ)OMP25 elicited specific antibodies to both SPPV and foreign genes VP1 and OMP25. Thus, SPPV NISKHI may be used as a potential safe immunogenic viral vector for the development of polyvalent vaccines.
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García-Sureda, Laura, Antonio Doménech-Sánchez, Mariette Barbier, Carlos Juan, Joan Gascó, and Sebastián Albertí. "OmpK26, a Novel Porin Associated with Carbapenem Resistance in Klebsiella pneumoniae." Antimicrobial Agents and Chemotherapy 55, no. 10 (August 1, 2011): 4742–47. http://dx.doi.org/10.1128/aac.00309-11.

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ABSTRACTClinical isolates ofKlebsiella pneumoniaeresistant to carbapenems are being isolated with increasing frequency. Loss of the expression of the major nonspecific porins OmpK35/36 is a frequent feature in these isolates. In this study, we looked for porins that could compensate for the loss of the major porins in carbapenem-resistant organisms. Comparison of the outer membrane proteins from twoK. pneumoniaeclinical isogenic isolates that are susceptible (KpCS-1) and resistant (KpCR-1) to carbapenems revealed the absence of OmpK35/36 and the presence of a new 26-kDa protein in the resistant isolate. An identical result was obtained when another pair of isogenic isolates that are homoresistant (Kpn-3) and heteroresistant (Kpn-17) to carbapenems were compared. Mass spectrometry and DNA sequencing analysis demonstrated that this new protein, designated OmpK26, is a small monomeric oligogalacturonate-specific porin that belongs to the KdgM family of porins. Insertion-duplication mutagenesis of the OmpK26 coding gene,yjhA, in the carbapenem-resistant, porin-deficient isolate KpCR-1 caused the expression of OmpK36 and the reversion to the carbapenem-susceptible phenotype, suggesting that OmpK26 is indispensable for KpCR-1 to lose OmpK36 and become resistant to these antibiotics. Moreover, loss of the major porin and expression of OmpK26 reducedin vitrofitness and attenuated virulence in a murine model of acute systemic infection. Altogether, these results indicate that expression of the oligogalacturonate-specific porin OmpK26 compensates for the absence of OmpK35/36 and allows carbapenem resistance inK. pneumoniaebut cannot restore the fitness of the microorganism.
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Noh, Susan M., Kelly A. Brayton, Donald P. Knowles, Joseph T. Agnes, Michael J. Dark, Wendy C. Brown, Timothy V. Baszler, and Guy H. Palmer. "Differential Expression and Sequence Conservation of the Anaplasma marginale msp2 Gene Superfamily Outer Membrane Proteins." Infection and Immunity 74, no. 6 (June 2006): 3471–79. http://dx.doi.org/10.1128/iai.01843-05.

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ABSTRACT Bacterial pathogens in the genera Anaplasma and Ehrlichia encode a protein superfamily, pfam01617, which includes the predominant outer membrane proteins (OMPs) of each species, major surface protein 2 (MSP2) and MSP3 of Anaplasma marginale and Anaplasma ovis, Anaplasma phagocytophilum MSP2 (p44), Ehrlichia chaffeensis p28-OMP, Ehrlichia canis p30, and Ehrlichia ruminantium MAP1, and has been shown to be involved in both antigenic variation within the mammalian host and differential expression between the mammalian and arthropod hosts. Recently, complete sequencing of the A. marginale genome has identified an expanded set of genes, designated omp1-14, encoding new members of this superfamily. Transcriptional analysis indicated that, with the exception of the three smallest open reading frames, omp2, omp3, and omp6, these superfamily genes are transcribed in A. marginale-infected erythrocytes, tick midgut and salivary glands, and the IDE8 tick cell line. OMPs 1, 4, 7 to 9, and 11 were confirmed to be expressed as proteins by A. marginale within infected erythrocytes, with expression being either markedly lower (OMPs 1, 4, and 7 to 9) or absent (OMP11) in infected tick cells, which reflected regulation at the transcript level. Although the pfam01617 superfamily includes the antigenically variable MSP2 and MSP3 surface proteins, analysis of the omp1-14 sequences throughout a cycle of acute and persistent infection in the mammalian host and tick transmission reveals a high degree of conservation, an observation supported by sequence comparisons between the St. Maries strain and Florida strain genomes.
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36

Zhu, Huapei, Hanwei Jiao, Xin Nie, Baobao Li, Kailian Xu, Feng Pang, Ruiyong Cao, et al. "Alterations of microRNAs and their predicted targeting mRNAs expression in RAW264.7 macrophages infected with Omp25 mutant Brucella melitensis." Innate Immunity 24, no. 6 (August 2018): 382–89. http://dx.doi.org/10.1177/1753425918792298.

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Brucellosis is a worldwide zoonosis caused by Brucella species and represents a serious threat to both human and animal health. Omp25 is an important immunogenic and protective antigen in Brucella species; however, the functional mechanism of Omp25 in macrophages has not yet been elucidated. Here, we constructed a Brucella melitensis omp25 deletion mutant (M5-90-Δ omp25) and performed microRNA (miRNA) profiling of infected RAW264.7 cells. Eight differentially expressed miRNAs ( mmu-miR-146a-5p, mmu-miR-155-5p, mmu-miR-3473a, mmu-miR-149-3p, mmu-miR-671-5p, mmu-miR-1224-5p, mmu-miR-1895, and mmu-miR-5126) were identified, with quantitative real-time PCR (qRT-PCR) analysis confirming the up-regulation of mmu-miR-146-a-5p and mmu-miR-155-5p and down-regulation of mmu-miR-149-3p and mmu-miR-5126. mRNA profiling of B. melitensis M5-90-Δo mp25-infected RAW264.7 cells identified 967 differentially expressed genes (DEGs) (fold change ≥ 2). Among these, we focused on genes that were predicted by TargetScan, miRanda, and PicTar to be the potential targets of the differentially expressed miRNAs. The results suggested that 17 separate genes are potentially targeted by mmu-miR-149-3p, with one of these genes, Tbr1, also targeted by mmu-miR-5126. qRT-PCR analysis confirmed the up-regulation of nine of the predicted target genes. Our findings provide important information about the functional molecules in host cells, including miRNA and their target genes, affected by Omp25 from Brucella. This information is particularly valuable for the prophylaxis and treatment of brucellosis.
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37

Ciervo, Alessandra, Paolo Visca, Andrea Petrucca, Luigi Maria Biasucci, Attilio Maseri, and Antonio Cassone. "Antibodies to 60-Kilodalton Heat Shock Protein and Outer Membrane Protein 2 of Chlamydia pneumoniae in Patients with Coronary Heart Disease." Clinical and Vaccine Immunology 9, no. 1 (January 2002): 66–74. http://dx.doi.org/10.1128/cdli.9.1.66-74.2002.

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ABSTRACT Evidence linking Chlamydia pneumoniae infection to atherosclerosis and to atherothrombotic events has recently emerged. A primary candidate implicated in these pathogenetic events is the 60-kDa chlamydial heat shock protein (HSP60). Another putative candidate to activate a potential proinflammatory mechanism is the chlamydial outer membrane protein 2 (OMP2). We have generated both HSP60 and OMP2 recombinant antigens in a nondenatured form and shown that (i) the two antigens were highly immunogenic in mice and (ii) murine antisera thus generated recognized the native C. pneumoniae proteins. We measured by enzyme linked immunosorbent assay (ELISA) and immunoblot assay antibody titers to the recombinant antigens in samples from 219 patients with coronary heart disease (CHD), 179 patients with unstable angina (UA), 40 patients with acute myocardial infarction (AMI), and 100 age-, sex-, and risk factor-matched healthy controls. We also examined whether anti-HSP60 and/or anti-OMP2 antibodies correlated with anti-C. pneumoniae antibodies assessed by a commercial microimmunofluorescence (MIF) assay. Immunoglobulin G (IgG), but neither IgA nor IgM, antibodies against the two recombinant proteins were detected by ELISA. In particular, anti-HSP60 antibodies were detected in >99% of CHD patients versus 0% of the controls, whereas the proportions of anti-OMP2 positive subjects were >70 and 27%, respectively. Nonetheless, among CHD patients, similar frequencies of positive subjects and titers of anti-HSP60 or anti-OMP2 antibodies were present in UA and AMI subjects. The anti-OMP2, but not the anti-HSP60, antibodies showed high specificity. Consistently, high serological correlation was observed between IgG MIF titers and IgG ELISA reactivity to OMP2 but not to HSP60. Overall, the results of this study demonstrate a strong correlation between CHD and anti-HSP60 IgG levels, as measured by our in-house ELISA. They also suggest that recombinant OMP2 ELISA, because of its high specificity and strong correlation with MIF assay, could be a candidate diagnostic marker for C. pneumoniae infection, which would be of potential usefulness for its specificity and nonsubjective nature.
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38

Komatsuzawa, Hitoshi, Toshihisa Kawai, Mark E. Wilson, Martin A. Taubman, Motoyuki Sugai, and Hidekazu Suginaka. "Cloning of the Gene Encoding the Actinobacillus actinomycetemcomitans Serotype b OmpA-Like Outer Membrane Protein." Infection and Immunity 67, no. 2 (February 1, 1999): 942–45. http://dx.doi.org/10.1128/iai.67.2.942-945.1999.

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ABSTRACT The gene encoding an outer membrane protein A (OmpA)-like, heat-modifiable Omp of Actinobacillus actinomycetemcomitans ATCC 43718 (strain Y4, serotype b) was cloned by a PCR cloning procedure. DNA sequence analysis revealed that the gene encodes a protein of 346 amino acid residues with a molecular mass of 36.9 kDa. The protein expressed by the cloned gene reacted with a monoclonal antibody to the previously described 29-kDa Omp (Omp29) of strain Y4. This monoclonal antibody reacted specifically with Omp29 of A. actinomycetemcomitans (serotype b), but not with any Omp of Escherichia coli, including OmpA. This protein exhibited characteristic heat modifiability on sodium dodecyl sulfate-polyacrylamide gels, showing an apparent molecular mass of 29 kDa when unheated and a mass of 34 kDa when heated. The N-terminal amino acid sequence of the protein expressed inE. coli perfectly matched those deduced from the purified Omp29 of strain Y4. The deduced amino acid sequence of the gene coding for Omp29 from serotype b matched completely (except for valine at position 321) that of a recently reported omp34gene described for A. actinomycetemcomitans serotype c (NCTC 9710). Because of the conserved nature of the gene within these serotypes, we designated the gene described herein from serotype b asomp34.
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Tibor, Anne, Béatrice Decelle, and Jean-Jacques Letesson. "Outer Membrane Proteins Omp10, Omp16, and Omp19 of Brucella spp. Are Lipoproteins." Infection and Immunity 67, no. 9 (September 1, 1999): 4960–62. http://dx.doi.org/10.1128/iai.67.9.4960-4962.1999.

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ABSTRACT The deduced sequences of the Omp10, Omp16, and Omp19 outer membrane proteins of Brucella spp. contain a potential bacterial lipoprotein processing sequence. After extraction with Triton X-114, these three proteins partitioned into the detergent phase. Processing of the three proteins is inhibited by globomycin, a specific inhibitor of lipoprotein signal peptidase. The three proteins were radioimmunoprecipitated from [3H]palmitic acid-labeledBrucella abortus lysates with monoclonal antibodies. These results demonstrate that Omp10, Omp16, and Omp19 are lipoproteins.
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40

Inui, Masafumi, and Makoto Asashima. "Identification and characterization of Xenopus OMP25." Development, Growth and Differentiation 46, no. 5 (October 2004): 405–12. http://dx.doi.org/10.1111/j.1440-169x.2004.00757.x.

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41

Mukherjee, Falguni, Jainendra Jain, Vipul Patel, and Mrinalini Nair. "Multiple genus-specific markers in PCR assays improve the specificity and sensitivity of diagnosis of brucellosis in field animals." Journal of Medical Microbiology 56, no. 10 (October 1, 2007): 1309–16. http://dx.doi.org/10.1099/jmm.0.47160-0.

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Brucella-specific nucleotide sequences encoding the BCSP 31 kDa protein, Omp2 and the 16S rRNA were employed in three independent diagnostic PCR assays. Results of the three PCR assays on six reference strains of Brucella were in complete agreement. The results of PCR assays based on bcsp and omp2 on 19 Indian field isolates (human, bovine and murine tissues) also agreed completely. However, when the 16S rRNA gene was employed as the diagnostic target in the PCR, only 14 out of these 19 isolates and 2 out of 7 bovine milk isolates were identified as the genus Brucella. The bovine blood samples were insensitive to 16S rRNA PCR. The antibody-detecting ELISA results of field samples (n=87) from a serologically positive herd in India were compared separately with omp2 and bcsp PCRs of blood (n=62). While the bcsp PCR was the most sensitive, the degree of association of ELISA with omp2 blood PCR (κ=0.37 at P <0.05) was similar to that with the bcsp blood PCR (κ =0.34 at P <0.05). An improvement in the correlation between ELISA and blood PCR was noticed (κ =0.5 at P <0.05) when a consensus result of omp2 and bcsp blood PCR was considered for comparison with ELISA. The use of more than one marker-based PCR gave increased sensitivity and higher specificity and appears to be a more reliable molecular diagnostic approach for screening of field animals.
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42

Billard, Elisabeth, Jacques Dornand, and Antoine Gross. "Brucella suis Prevents Human Dendritic Cell Maturation and Antigen Presentation through Regulation of Tumor Necrosis Factor Alpha Secretion." Infection and Immunity 75, no. 10 (July 16, 2007): 4980–89. http://dx.doi.org/10.1128/iai.00637-07.

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ABSTRACT Brucella is a facultative intracellular pathogen and the etiological agent of brucellosis. In some cases, human brucellosis results in a persistent infection that may reactivate years after the initial exposure. The mechanisms by which the parasite evades clearance by the immune response to chronically infect its host are unknown. We recently demonstrated that dendritic cells (DCs), which are critical components of adaptive immunity, are highly susceptible to Brucella infection and are a preferential niche for the development of the bacteria. Here, we report that in contrast to several intracellular bacteria, Brucella prevented the infected DCs from engaging in their maturation process and impaired their capacities to present antigen to naïve T cells and to secrete interleukin-12. Moreover, Brucella-infected DCs failed to release tumor necrosis factor alpha (TNF-α), a defect involving the bacterial protein Omp25. Exogenous TNF-α addition to Brucella-infected DCs restored cell maturation and allowed them to present antigens. Two avirulent mutants of B. suis, B. suis bvrR and B. suis omp25 mutants, which do not express the Omp25 protein, triggered TNF-α production upon DC invasion. Cells infected with these mutants subsequently matured and acquired the ability to present antigens, two properties which were dramatically impaired by addition of anti-TNF-α antibodies. In light of these data, we propose a model in which virulent Brucella alters the maturation and functions of DCs through Omp25-dependent control of TNF-α production. This model defines a specific evasion strategy of the bacteria by which they can escape the immune response to chronically infect their host.
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43

Puig, Marta, Carme Fusté, and Miquel Viñas. "Outer membrane proteins from Serratia marcescens." Canadian Journal of Microbiology 39, no. 1 (January 1, 1993): 108–11. http://dx.doi.org/10.1139/m93-015.

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The outer membrane proteins (OMPs) of several strains of Serratia marcescens have been studied by sodium dodecyl sulphate – urea – polyacrylamide gel electrophoresis. Four major OMPs, named Omp1, Omp2, Omp3, and OmpA (42, 40, 39, and 37 kDa, respectively), have been visualized. The relative proportions of Omp2 and Omp3 depend on cultural conditions (temperature of incubation, osmolarity, and nutrient availability).Key words: Serratia marcescens, outer membrane proteins, porin.
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44

Bulashev, Aitbay, Orken Akibekov, Alfiya Syzdykova, Zhanbolat Suranshiyev, and Bakytkali Ingirbay. "Use of recombinant Brucella outer membrane proteins 19, 25, and 31 for serodiagnosis of bovine brucellosis." July-2020 13, no. 7 (2020): 1439–47. http://dx.doi.org/10.14202/vetworld.2020.1439-1447.

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Background and Aim: Brucellosis remains one of the most common zoonoses. The current anti-brucellosis measures are largely deemed ineffective due to a lack of specificity of conventional serological tests. This study evaluated the use of Brucella outer membrane protein (Omp)19 for serodiagnostic testing. Materials and Methods: The antigenicity of recombinant Brucella Omp19, Omp25, and Omp31 was examined in serum samples from mice and rabbits immunized with Omp19 or Brucella abortus 19 whole cell (WC) and 12 and 152 cows experimentally or naturally infected with brucellosis, respectively. Serum samples were collected from 151 cows that were vaccinated with B. abortus 19 and 12 unvaccinated heifers that were maintained on a brucellosis-free farm. Results: Immunization with Omp19 resulted in antibody production in mice after a single injection without the use of adjuvant. Serum antibodies obtained from rabbits immunized with inactivated B. abortus strain 19 WC targeted Omps by enzyme-linked immunosorbent assay (ELISA) and Western blot. Antibodies targeting Omp19 were identified in all B. abortus strain 544 experimentally infected cows at day 14 post-inoculation (p.i.); Omp25 was detected by ELISA at day 28 p.i., while an ELISA targeting Omp31 was negative for 25% of cows at this time point. Omp19 and Omp25 were readily detected by sera from cows from a new epizootic focus. Antibodies recognizing Omps were also detected in >50% of the animals maintained in a brucellosis-free herd at 10 months after vaccination. Conclusion: Brucella Omp19 in combination with Omp25 and Omp31 may be utilized as target antigens in an ELISA designed for serological testing of unvaccinated cattle.
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Zhang, Junbo, Fei Guo, Xiaoqiang Huang, Chuangfu Chen, Ruitian Liu, Hui Zhang, Yuanzhi Wang, Shuanghong Yin, and Zhiqiang Li. "A novel Omp25-binding peptide screened by phage display can inhibit Brucella abortus 2308 infection in vitro and in vivo." Journal of Medical Microbiology 63, no. 6 (June 1, 2014): 780–87. http://dx.doi.org/10.1099/jmm.0.069559-0.

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Brucellosis is a globally distributed zoonotic disease affecting animals and humans, and current antibiotic and vaccine strategies are not optimal. The surface-exposed protein Omp25 is involved in Brucella virulence and plays an important role in Brucella pathogenesis during infection, suggesting that Omp25 could be a useful target for selecting potential therapeutic molecules to inhibit Brucella pathogenesis. In this study, we identified, we believe for the first time, peptides that bind specifically to the Omp25 protein of pathogens, using a phage panning technique, After four rounds of panning, 42 plaques of eluted phages were subjected to pyrosequencing. Four phage clones that bound better than the other clones were selected following confirmation by ELISA and affinity constant determination. The peptides selected could significantly inhibit Brucella abortus 2308 (S2308) internalization and intracellular growth in RAW264.7 macrophages, and significantly induce secretion of TNF-α and IL-12 in peptide- and S2308-treated cells. Any observed peptide (OP11, OP27, OP35 or OP40) could significantly inhibit S2308 infection in BALB/c mice. Moreover, the peptide OP11 was the best candidate peptide for inhibiting S2308 infection in vitro and in vivo. These results suggest that peptide OP11 has potential for exploitation as a peptide drug in resisting S2308 infection.
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46

Whatmore, Adrian M., Nicholas Davison, Axel Cloeckaert, Sascha Al Dahouk, Michel S. Zygmunt, Simon D. Brew, Lorraine L. Perrett, et al. "Brucella papionis sp. nov., isolated from baboons (Papio spp.)." International Journal of Systematic and Evolutionary Microbiology 64, Pt_12 (December 1, 2014): 4120–28. http://dx.doi.org/10.1099/ijs.0.065482-0.

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Two Gram-negative, non-motile, non-spore-forming coccoid bacteria (strains F8/08-60T and F8/08-61) isolated from clinical specimens obtained from baboons (Papio spp.) that had delivered stillborn offspring were subjected to a polyphasic taxonomic study. On the basis of 16S rRNA gene sequence similarities, both strains, which possessed identical sequences, were assigned to the genus Brucella . This placement was confirmed by extended multilocus sequence analysis (MLSA), where both strains possessed identical sequences, and whole-genome sequencing of a representative isolate. All of the above analyses suggested that the two strains represent a novel lineage within the genus Brucella . The strains also possessed a unique profile when subjected to the phenotyping approach classically used to separate species of the genus Brucella, reacting only with Brucella A monospecific antiserum, being sensitive to the dyes thionin and fuchsin, being lysed by bacteriophage Wb, Bk2 and Fi phage at routine test dilution (RTD) but only partially sensitive to bacteriophage Tb, and with no requirement for CO2 and no production of H2S but strong urease activity. Biochemical profiling revealed a pattern of enzyme activity and metabolic capabilities distinct from existing species of the genus Brucella . Molecular analysis of the omp2 locus genes showed that both strains had a novel combination of two highly similar omp2b gene copies. The two strains shared a unique fingerprint profile of the multiple-copy Brucella-specific element IS711. Like MLSA, a multilocus variable number of tandem repeat analysis (MLVA) showed that the isolates clustered together very closely, but represent a distinct group within the genus Brucella . Isolates F8/08-60T and F8/08-61 could be distinguished clearly from all known species of the genus Brucella and their biovars by both phenotypic and molecular properties. Therefore, by applying the species concept for the genus Brucella suggested by the ICSP Subcommittee on the Taxonomy of Brucella, they represent a novel species within the genus Brucella , for which the name Brucella papionis sp. nov. is proposed, with the type strain F8/08-60T ( = NCTC 13660T = CIRMBP 0958T).
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47

Silva-Zacarias, Francielle Gibson da, Amauri Alcindo Alfieri, Kledir Anderson Hofstaetter Spohr, Bruna Azevedo de Carvalho Lima, Fábio Juliano Negrão, Michele Lunardi, and Julio Cesar de Freitas. "Validation of a PCR Assay for Chlamydophila abortus rRNA gene detection in a murine model." Brazilian Archives of Biology and Technology 52, spe (November 2009): 99–106. http://dx.doi.org/10.1590/s1516-89132009000700014.

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Chlamydophila abortus (C. abortus) is associated with reproductive problems in cattle, sheep, and goats. Diagnosis of C. abortus using embryonated chicken eggs or immortalized cell lines has a very low sensitivity. Polymerase chain reaction (PCR) assays have been used to detect C. abortus infection in clinical specimens and organ fragments, such as placenta, fetal organs, vaginal secretions, and semen. The aim of this study was to develop a PCR assay for the amplification of an 856-bp fragment of the rRNA gene of the Chlamydiaceae family. The PCR assay was evaluated using organs from 15 mice experimentally infected with the S26/3 reference strain of C. abortus. The results of the rRNA PCR were compared to the results from another PCR system (Omp2 PCR) that has been previously described for the Omp2 (outer major protein) gene from the Chlamydiaceae family. From the 15 C. abortus-inoculated mice, 13 (K=0.84, standard error =0.20) tested positive using the rRNA PCR assay and 9 (K=0.55, standard error=0.18) tested positive using the Omp2 PCR assay. The detection limit, measured using inclusion-forming units (IFU), for C. abortus with the rRNA PCR (1.05 IFU) was 100-fold lower than for the Omp2 PCR (105 IFU). The higher sensitivity of the rRNA PCR, as compared to the previously described PCR assay, and the specificity of the assay, demonstrated using different pathogenic microorganisms of the bovine reproductive system, suggest that the new PCR assay developed in this study can be used for the molecular diagnosis of C. abortus in abortion and other reproductive failures in bovines, caprines, and ovines.
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48

Airaksinen, Ulla, Tuula Penttilä, Eva Wahlström, Jenni M. Vuola, Mirja Puolakkainen, and Matti Sarvas. "Production of Chlamydia pneumoniae Proteins in Bacillus subtilis and Their Use in Characterizing Immune Responses in the Experimental Infection Model." Clinical Diagnostic Laboratory Immunology 10, no. 3 (May 2003): 367–75. http://dx.doi.org/10.1128/cdli.10.3.367-375.2003.

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ABSTRACT Due to intracellular growth requirements, large-scale cultures of chlamydiae and purification of its proteins are difficult and laborious. To overcome these problems we produced chlamydial proteins in a heterologous host, Bacillus subtilis, a gram-positive nonpathogenic bacterium. The genes of Chlamydia pneumoniae major outer membrane protein (MOMP), the cysteine-rich outer membrane protein (Omp2), and the heat shock protein (Hsp60) were amplified by PCR, and the PCR products were cloned into expression vectors containing a promoter, a ribosome binding site, and a truncated signal sequence of the α-amylase gene from Bacillus amyloliquefaciens. C. pneumoniae genes were readily expressed in B. subtilis under the control of the α-amylase promoter. The recombinant proteins MOMP and Hsp60 were purified from the bacterial lysate with the aid of the carboxy-terminal histidine hexamer tag by affinity chromatography. The Omp2 was separated as an insoluble fraction after 8 M urea treatment. The purified proteins were successfully used as immunogens and as antigens in serological assays and in a lymphoproliferation test. The Omp2 and Hsp60 antigens were readily recognized by the antibodies appearing after pulmonary infection following intranasal inoculation of C. pneumoniae in mice. Also, splenocytes collected from mice immunized with MOMP or Hsp60 proteins proliferated in response to in vitro stimulation with the corresponding proteins.
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Cloeckaert, Axel, Anne Tibor, and Michel S. Zygmunt. "Brucella Outer Membrane Lipoproteins Share Antigenic Determinants with Bacteria of the FamilyRhizobiaceae." Clinical Diagnostic Laboratory Immunology 6, no. 4 (July 1, 1999): 627–29. http://dx.doi.org/10.1128/cdli.6.4.627-629.1999.

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ABSTRACT Brucellae have been reported to be phylogenetically related to bacteria of the family Rhizobiaceae. In the present study, we used a panel of monoclonal antibodies (MAbs) to Brucellaouter membrane proteins (OMPs) to determine the presence of common OMP epitopes in some representative bacteria of this family, i.e.,Ochrobactrum anthropi, Phyllobacterium rubiacearum, Rhizobium leguminosarum, andAgrobacterium tumefaciens, and also in bacteria reported to serologically cross-react with brucella, i.e., Yersinia enterocolitica O:9, Escherichia coli O:157, andSalmonella urbana. In particular, most MAbs to theBrucella outer membrane lipoproteins Omp10, Omp16, and Omp19 cross-reacted with O. anthropi and P. rubiacearum, which are actually the closest relatives of brucellae. Some of them also cross-reacted, but to a lower extent, withR. leguminosarum and A. tumefaciens. The putative Omp16 and Omp19 homologs in these bacteria showed the same apparent molecular masses as their Brucella counterparts. None of the antilipoprotein MAbs cross-reacted with Y. enterocolitica O:9, E. coli O:157, or S. urbana.
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50

Kaushik, P., P. Chaudhury, G. Shukla, and D. K. Singh. "Immunogenicity of Recombinant Omp28 from Brucella Melitensis in Mice." International Journal of Infectious Diseases 12 (December 2008): e252. http://dx.doi.org/10.1016/j.ijid.2008.05.683.

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