Relevant bibliographies by topics / Catarrhalis

Academic literature on the topic 'Catarrhalis'

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Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "Catarrhalis"

1

Yang, Min, Antoinette Johnson, and Timothy F. Murphy. "Characterization and Evaluation of theMoraxella catarrhalisOligopeptide Permease A as a Mucosal Vaccine Antigen." Infection and Immunity 79, no. 2 (December 6, 2010): 846–57. http://dx.doi.org/10.1128/iai.00314-10.

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ABSTRACTMoraxella catarrhalisis a common cause of otitis media in children and of lower respiratory tract infections in adults with chronic obstructive pulmonary disease; therefore, these two groups would benefit from a vaccine to preventM. catarrhalisinfections. A genome mining approach for vaccine antigens identified oligopeptide permease protein A (OppA), an oligopeptide binding protein of an apparent oligopeptide transport system. Analysis of theoppAgene by PCR and sequence analysis revealed that OppA is highly conserved among clinical isolates ofM. catarrhalis. Recombinant OppA was expressed as a lipoprotein and purified, and anoppAknockout mutant was constructed. Antiserum raised to recombinant purified OppA recognized epitopes on the bacterial surface of the wild type but not the OppA knockout mutant. Antibodies raised to purified recombinant OppA recognized native OppA in multiple strains. Intranasal immunization of mice induced systemic and mucosal antibodies to OppA and resulted in enhanced clearance ofM. catarrhalisin a mouse pulmonary clearance model. OppA is a highly conserved, immunogenic protein that expresses epitopes on the bacterial surface and that induces potentially protective immune responses in a mouse model. OppA should be evaluated further as a vaccine antigen forM. catarrhalis.
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Aebi, Christoph, Leslie D. Cope, Jo L. Latimer, Sharon E. Thomas, Clive A. Slaughter, George H. McCracken, and Eric J. Hansen. "Mapping of a Protective Epitope of the CopB Outer Membrane Protein of Moraxella catarrhalis." Infection and Immunity 66, no. 2 (February 1, 1998): 540–48. http://dx.doi.org/10.1128/iai.66.2.540-548.1998.

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ABSTRACT A monoclonal antibody (MAb) (MAb 10F3) directed against the CopB outer membrane protein of Moraxella catarrhalis previously was found to enhance pulmonary clearance of M. catarrhalisin an animal model (M. Helminen, I. Maciver, J. L. Latimer, L. D. Cope, G. H. McCracken, Jr., and E. J. Hansen, Infect. Immun. 61:2003–2010, 1993). In the present study, this same MAb was shown to exert complement-dependent bactericidal activity against this pathogen in vitro. Nucleotide sequence analysis of thecopB gene from two MAb 10F3-reactive and two MAb 10F3-unreactive strains of M. catarrhalis revealed that the deduced amino acid sequences of these four CopB proteins were at least 90% identical. Comparison of the amino acid sequences of these proteins allowed localization of possible MAb 10F3 binding sites to five relatively small regions of the CopB protein from M. catarrhalis O35E. When five synthetic peptides representing these regions were tested for their ability to bind MAb 10F3 in a direct enzyme-linked immunosorbent assay system, an oligopeptide containing 26 amino acids was shown to bind this MAb. The actual binding region for MAb 10F3 was localized further through the use of overlapping decapeptides that spanned this 26-mer. A fusion protein containing the same 26-mer readily bound MAb 10F3 and was used to immunize mice. The resultant antiserum contained antibodies that reacted with the CopB protein of the homologous M. catarrhalis strain in Western blot analysis and bound to the surface of both homologous and heterologous strains of M. catarrhalis.
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3

Riou, J. Y., and M. Guibourdenche. "Branhamella catarrhalis." Drugs 31, Supplement 3 (1986): 1–6. http://dx.doi.org/10.2165/00003495-198600313-00003.

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SHEFF, BARBARA. "Moraxella Catarrhalis." Nursing 33, no. 1 (January 2003): 81. http://dx.doi.org/10.1097/00152193-200301000-00055.

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5

Otsuka, Taketo, Charmaine Kirkham, Aimee Brauer, Mary Koszelak-Rosenblum, Michael G. Malkowski, and Timothy F. Murphy. "The Vaccine Candidate Substrate Binding Protein SBP2 Plays a Key Role in Arginine Uptake, Which Is Required for Growth of Moraxella catarrhalis." Infection and Immunity 84, no. 2 (November 23, 2015): 432–38. http://dx.doi.org/10.1128/iai.00799-15.

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Moraxella catarrhalisis an exclusively human pathogen that is an important cause of otitis media in children and lower respiratory tract infections in adults with chronic obstructive pulmonary disease. A vaccine to preventM. catarrhalisinfections would have an enormous global impact in reducing morbidity resulting from these infections. Substrate binding protein 2 (SBP2) of an ABC transporter system has recently been identified as a promising vaccine candidate antigen on the bacterial surface ofM. catarrhalis. In this study, we showed that SBP1, -2, and -3 individually bind different basic amino acids with exquisite specificity. We engineered mutants that each expressed a single SBP from this gene cluster and showed in growth experiments that SBP1, -2, and -3 serve a nutritional function through acquisition of amino acids for the bacterium. SBP2 mediates uptake of arginine, a strict growth requirement ofM. catarrhalis. Adherence and invasion assays demonstrated that SBP1 and SBP3 play a role in invasion of human respiratory epithelial cells, consistent with a nutritional role in intracellular survival in the human respiratory tract. This work demonstrates that the SBPs of an ABC transporter system function in the uptake of basic amino acids to support growth ofM. catarrhalis. The critical role of SBP2 in arginine uptake may contribute to its potential as a vaccine antigen.
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Sano, Naoto, Satoshi Matsunaga, Tomonori Akiyama, Yukari Nakashima, Koji Kusaba, Zenzo Nagasawa, Shunzo Koizumi, Masaaki Goto, and Hiroshi Miyamoto. "Moraxella catarrhalis bacteraemia associated with prosthetic vascular graft infection." Journal of Medical Microbiology 59, no. 2 (February 1, 2010): 245–50. http://dx.doi.org/10.1099/jmm.0.013789-0.

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Moraxella catarrhalis, formerly called Branhamella catarrhalis, ‘Neisseria catarrhalis’ or ‘Micrococcus catarrhalis’, is a Gram-negative, aerobic diplococcus frequently found as a colonizer of the upper respiratory tract. Over the last 20–30 years, this bacterium has emerged as a genuine pathogen, and is now considered an important cause of otitis media in children and an aetiological agent in pneumonia in adults with chronic obstructive pulmonary disease. However, bacteraemia due to M. catarrhalis has rarely been reported. Presented here is a case of M. catarrhalis bacteraemia associated with prosthetic vascular graft infection along with a review of the relevant literature.
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Slevogt, Hortense, Bernd Schmeck, Carola Jonatat, Janine Zahlten, Wiebke Beermann, Vincent van Laak, Bastian Opitz, et al. "Moraxella catarrhalis induces inflammatory response of bronchial epithelial cells via MAPK and NF-κB activation and histone deacetylase activity reduction." American Journal of Physiology-Lung Cellular and Molecular Physiology 290, no. 5 (May 2006): L818—L826. http://dx.doi.org/10.1152/ajplung.00428.2005.

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Moraxella catarrhalis is a major cause of infectious exacerbations of chronic obstructive lung disease (COPD) and may also contribute to the pathogenesis of COPD. Little is known about M. catarrhalis-bronchial epithelium interaction. We investigated activation of M. catarrhalis infected bronchial epithelial cells and characterized the signal transduction pathways. Moreover, we tested the hypothesis that the M. catarrhalis-induced cytokine expression is regulated by acetylation of histone residues and controlled by histone deacetylase activity (HDAC). We demonstrated that M. catarrhalis induced a strong time- and dose-dependent inflammatory response in the bronchial epithelial cell line (BEAS-2B), characterized by the release of IL-8 and GM-CSF. For this cytokine liberation activation of the ERK and p38 mitogen-activated protein (MAP) kinases and transcription factor NF-κB was required. Furthermore, M. catarrhalis-infected bronchial epithelial cells showed an enhanced acetylation of histone H3 and H4 globally and at the promoter of the il8 gene. Preventing histone deacetylation by the histone deacetylase inhibitor trichostatin A augmented the M. catarrhalis-induced IL-8 response. After exposure to M. catarrhalis, we found a decrease in global histone deacetylase expression and activity. Our findings suggest that M. catarrhalis-induced activation of il8 gene transcription was caused by interference with epigenetic mechanisms regulating il8 gene accessibility. Our findings provide insight into important molecular and cellular mechanisms of M. catarrhalis-induced activation of human bronchial epithelium.
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Igic, Marija, Ljiljana Kesic, Radmila Obradovic, Gordana Filipovic, Branislava Stojkovic, and Kosta Todorovic. "Comparative clinical evaluation of the therapeutic effects of low-level laser and hyaluronic acid on gingivitis catarrhalis in children." Vojnosanitetski pregled 77, no. 7 (2020): 736–39. http://dx.doi.org/10.2298/vsp171207118i.

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Background/Aim. Gingivitis catarrhalis is the most common disease of the oral mucosa in children, representing an inflammation of the gingiva of an exudative nature. The aim of this study was to evaluate the effectiveness of low-level laser therapy and hyaluronic acid therapy on gingivitis catarrhalis in children using the appropriate clinical parameters. Methods. The study involved 100 children with permanent dentition in whom gingivitis catarrhalis had been diagnosed. The examinees were divided into two groups: the group I consisting of patients with gingival inflammation (50 examinees) in whom the therapy with hyaluronic acid was applied after the removal of soft and hard dental deposits, and the group II consisting of patients with gingival inflammation (50 examinees) in whom low-level laser therapy was applied after the removal of soft and hard dental deposits. Clinical evaluation of the therapeutic effects of low-level laser and hyaluronic acid on gingivitis catarrhalis was performed using the appropriate indices: the Greene-Vermillion Plaque Index (PI), Muhlemann bleeding index (BI), and Community Periodontal Index of Treatment Needs (CPITN). Results. Using the Student?s t-test for dependent samples, a statistically significant difference was obtained (p < 0.001) between the PI, BI, and CPITN indices before and after the therapy in both examined groups. Moreover, the CPITN index after the therapy in the group II was statistically significantly lower (p < 0.05) than that obtained in the group I. Conclusion. The results demonstrated an exceptional effect of hyaluronic acid and low-level laser therapy, supplementing basic therapy, in the treatment of catarrhal gingivitis in children. Somewhat better results were achieved with the combination of basic therapy and low-level laser.
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Gutbier, Birgitt, Katja Fischer, Jan-Moritz Doehn, Carolin von Lachner, Christian Herr, Esther Klaile, Ursula Frischmann, et al. "Moraxella catarrhalisinduces an immune response in the murine lung that is independent of human CEACAM5 expression and long-term smoke exposure." American Journal of Physiology-Lung Cellular and Molecular Physiology 309, no. 3 (August 1, 2015): L250—L261. http://dx.doi.org/10.1152/ajplung.00265.2014.

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In patients with chronic obstructive pulmonary disease (COPD), Moraxella catarrhalis infection of the lower airways is associated with chronic colonization and inflammation during stable disease and acute exacerbations. Chronic smoke exposure induces chronic inflammation and impairs mucociliary clearance, thus contributing to bacterial colonization of the lower airways in COPD patients. The human-specific carcinoembryonic antigen-related cell adhesion molecule (CEACAM) 5, expressed in human airways, has been shown to contribute to epithelial colonization of CEACAM-binding pathogens. To investigate the impact of CEACAM5 expression on pulmonary M. catarrhalis colonization, we infected mice transgenic for human CEACAM5 (hCEACAM5) and wild type mice intratracheally with M. catarrhalis with or without preceding smoke exposure and analyzed bacterial colonization and local and systemic inflammation. Our results show that airway infection with M. catarrhalis accelerated acute local but not systemic inflammation, albeit independent of hCEACAM5 expression. Long-term smoke exposure alone or prior to M. catarrhalis infection did not contribute to increased local or systemic inflammation. No difference was found in pulmonary clearance of M. catarrhalis in hCEACAM5-transgenic mice compared with wild-type mice. Smoke exposure neither altered time nor extent of persistence of M. catarrhalis in the lungs of both genotypes. In conclusion, M. catarrhalis induced a local acute immune response in murine airways. Neither hCEACAM5 expression nor chronic smoke exposure nor a combination of both was sufficient as prerequisites for the establishment of chronic M. catarrhalis colonization. Our results demonstrate the difficulties in mirroring conditions of chronic airways colonization of M. catarrhalis in a murine model.
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Luke, Nicole R., Joseph A. Jurcisek, Lauren O. Bakaletz, and Anthony A. Campagnari. "Contribution of Moraxella catarrhalis Type IV Pili to Nasopharyngeal Colonization and Biofilm Formation." Infection and Immunity 75, no. 12 (October 1, 2007): 5559–64. http://dx.doi.org/10.1128/iai.00946-07.

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ABSTRACT Moraxella catarrhalis is a gram-negative mucosal pathogen of the human respiratory tract. Although little information is available regarding the initial steps of M. catarrhalis pathogenesis, this organism must be able to colonize the human mucosal surface in order to initiate an infection. Type IV pili (TFP), filamentous surface appendages primarily comprised of a single protein subunit termed pilin, play a crucial role in the initiation of disease by a wide range of bacteria. We previously identified the genes that encode the major proteins involved in the biosynthesis of M. catarrhalis TFP and determined that the TFP expressed by this organism are highly conserved and essential for natural transformation. We extended this initial study by investigating the contribution of TFP to the early stages of M. catarrhalis colonization. TFP-deficient M. catarrhalis bacteria exhibit diminished adherence to eukaryotic cells in vitro. Additionally, our studies demonstrate that M. catarrhalis cells form a mature biofilm in continuous-flow chambers and that biofilm formation is enhanced by TFP expression. The potential role of TFP in colonization by M. catarrhalis was further investigated using in vivo studies comparing the abilities of wild-type M. catarrhalis and an isogenic TFP mutant to colonize the nasopharynx of the chinchilla. These results suggest that the expression of TFP contributes to mucosal airway colonization. Furthermore, these data indicate that the chinchilla model of nasopharyngeal colonization provides an effective animal system for studying the early steps of M. catarrhalis pathogenesis.
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Dissertations / Theses on the topic "Catarrhalis"

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Enright, Mark Charles. "Molecular characterization of Moraxella catarrhalis." Thesis, University of Aberdeen, 1994. http://digitool.abdn.ac.uk:80/webclient/DeliveryManager?pid=158242.

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Moraxella catarrhalis is a gram-negative diplococcus which until recently was thought to be a harmless commensal. Increasing awareness has established the pathogenic nature of this organism and it is now recognised as a major cause of otitis media in children, exacerbations of chronic bronchitis in elderly patients and an occasional cause of invasive disease. M. catarrhalis is spread nosocomially especially in respiratory wards containing elderly patients. This study evaluated four methods for typing nosocomially spread isolates:- immunoblotting with normal human serum (NHS), and three DNA fingerprinting methods. The most discriminatory method found was restriction endonuclease analysis (REA) using Taq I, although immunoblotting with NHS and pulsed-field gel electrophoresis (PFGE) using Sma I sub-divided isolates grouped together by the other methods. PFGE using Not I only confirmed groupings made by other methods. A study of M. catarrhalis and phenotypically similar organisms was performed using comparisons of partial 16S rDNA sequence. 16S rDNA of M. catarrhalis strains from disparate geographical locations was found to be extremely conserved M. catarrhalis 16S rDNA was very similar to that of other Moraxella species whilst Moraxella species were found to be generally distinct from the Neisseria and Kingella species studied. These results confirm M. catarrhalis as a genuine member of the Moraxellae.
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Gill, Lyndell R. "Moraxella (Branhamella) Catarrhalis: A Molecular Epidemiology Study." Digital Commons @ East Tennessee State University, 1995. https://dc.etsu.edu/etd/2684.

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Moraxella (Branhamella) catarrhalis is the third-most-frequently isolated microorganism associated with acute exacerbations of chronic bronchitis in patients during their stay at the Mountain Home VA Medical Center (MHVAMC). In order to develop a practical, epidemiologically-meaningful typing method for M. (B.) catarrhalis, we tested two methods based on analysis of chromosomal DNA for typeability, reproducibility, and ability to differentiate between unrelated strains (discriminatory power, D). M. (B.) catarrhalis isolants from MHVAMC from 7/1/87-6/30/88 were grown overnight in broth and embedded in agarose. DNA was isolated by standard methods. The DNA was subjected to: (1) restriction endonuclease digestion (with either Bgl II or Pme I) followed by pulsed-field gel electrophoresis (PFGE) and (2) restriction endonuclease digestion (with Hae III), followed by horizontal gel electrophoresis, Southern transfer and hybridization with a M. (B.) catarrhalis-specific DNA probe (M46). Reliable and reproducible patterns were produced from 144 of 159 isolants (91%) using Hae III, 155 of 159 (97%) using Pme I, and all isolants using Bgl II. Three clusters of isolants, Groups A (n = 18), B (n = 18), and C (n = 12) were detected. Within each group, isolants were identical by all typing methods tested. Chart review revealed no apparent epidemiologic link for Group A, while in Group B, 16 of 18 patients were housed on two wards, and in Group C, all cases occurred within two months, suggesting epidemiologic links within Groups B and C. Comparisons of results from isolants from various wards and isolants from outpatients were used to determine D of each method. Digestion with Pme I followed by PFGE was the most discriminating technique (D = 0.978) followed by Bgl II with PFGE (D = 0.962), then M46 probe hybridization (D = 0.929). The restriction endonucleases Pme I and Bgl II were highly discriminating and useful in the epidemiologic typing of M. (B.) catarrhalis. While useful, the M46 probe following Hae III digestion was not as discriminating.
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Bullard, Brian. "Characterization of the Moraxella catarrhalis Hag Adhesin." University of Toledo Health Science Campus / OhioLINK, 2007. http://rave.ohiolink.edu/etdc/view?acc_num=mco1195596894.

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Stawska, Agnieszka A. "Purification of Aspartate Transcarbamoylase from Moraxella (Branhamella) catarrhalis." Thesis, University of North Texas, 2001. https://digital.library.unt.edu/ark:/67531/metadc2864/.

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The enzyme, aspartate transcarbamoylase (ATCase) from Moraxella (Branhamella) catarrhalis, has been purified. The holoenzyme has a molecular mass of approximately 510kDa, harbors predominantly positive charges and is hydrophobic in nature. The holoenzyme possesses two subunits, a smaller one of 40 kDa and a larger one of 45 kDa. A third polypeptide has been found to contribute to the overall enzymatic activity, having an approximate mass of 55 kDa. The ATCase purification included the generation of cell-free extract, streptomycin sulfate cut, 60 °C heat step, ammonium sulfate cut, dialysis and ion, gel-filtration and hydrophobic interaction chromatography. The enzyme's performance throughout purification steps was analyzed on activity and SDS-PAGE gradient gels. Its enzymatic, specific activities, yield and fold purification, were also determined.
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Attia, Ahmed Sherif. "The USPA2 protein and serum resistance of Moraxella Catarrhalis." Access to abstract only; dissertation is embargoed until after 5/15/2007, 2006. http://www4.utsouthwestern.edu/library/ETD/etdDetails.cfm?etdID=145.

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Fowler, Michael A. (Michael Allen) 1961. "Characterization of Aspartate Transcarbamoylase and Dihydroorotase in Moraxella Catarrhalis." Thesis, University of North Texas, 1998. https://digital.library.unt.edu/ark:/67531/metadc277709/.

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Bacterial aspartate transcarbamoylases (ATCase's) are divided into three classes that correspond to taxonomic relationships within the bacteria. The opportunistic pathogen Moraxeila catarrhalis has undergone several reclassifications based on traditional microbiological criteria. The previously uncharacterized ATCase from M. catarrhalis was purified to homogeneity and its chemical properties characterized. The ATCase from M. catarrhalis is a class C ATCase with an apparent molecular mass of 480-520 kDa. The M. catarrhalis ATCase is a dodecomer composed of six 35 kDa polypeptides and six 45 kDa polypeptides. The enzyme has an unusually high pH optimum of greater than pH 10. The enzyme exhibited hyperbolic kinetic with a Km for aspartate of 2 mM. A single, separate 78 kDa dihydroorotase from M. catarrhalis was identified and it was not associated with ATCase. These data support the reclassification of M. catarrhalis out of the Neisseriaceae family.
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Bowman, Melissa Lynne. "Biochemical characterization of Moraxella catarrhalis strains associated with Otitis media." Thesis, Georgia Institute of Technology, 2001. http://hdl.handle.net/1853/25397.

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Easton, Donna Meredith, and n/a. "Functional and Antigenic Characterisation of the Moraxella catarrhalis protein M35." University of Canberra. n/a, 2008. http://erl.canberra.edu.au./public/adt-AUC20081217.083105.

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This thesis reports the characterisation of a novel outer membrane protein (OMP) from M. catarrhalis, designated M35, with a molecular mass of 36.1 kDa. This protein is structurally homologous to classic Gram-negative porins, such as OMP C from E. coli and OMP K36 from K. pneumoniae, with a predicted structure of 8 surface loops connecting 16 antiparallel -sheets. Comparison of the DNA sequences of the M35 genes from 18 diverse clinical isolates showed that the gene was highly conserved (99.6-100 % of nucleotides) with only one isolate (ID78LN266) having base variations that resulted in amino acid substitutions. A single amino acid mutation in the 3rd external loop of M35 in isolate ID78LN266 significantly affected antibody recognition, indicating that loop 3 contains an immunodominant B-cell epitope. The reduction in antibody-binding to M35 from ID78LN266 was similar to that caused by complete removal of loop 3. Since loop 3 folds into the porin channel in the classic structure, the antibody specificity to loop 3 was hypothesised to be a potential mechanism for evasion of host immune responses targeted to M35, potentially explaining the high degree of conservation across isolates. A series of recombinant proteins were constructed to analyse the binding to M35 of antibodies specificity for loop 3 or the remainder of the protein. It was found that loop 3- specific antibodies were not able to bind to M35 on the surface of M. catarrhalis and that this corresponds both with a lack of ability to enhance opsonophagocytosis in vitro and bacterial clearance in vivo. Additionally, antibodies raised against a version of M35 lacking loop 3 and M35 from the variant isolate ID78LN266 were both no less effective than the full consensus M35 by both these measures. It therefore appears that while the majority of antibodies raised against M35 are specific for loop 3 these antibodies do not mediate anti-M. catarrhalis actions. Two deletion mutant strains of M. catarrhalis that do not contain the outer membrane protein M35 were created by insertional inactivation of the M35 gene. Growth comparisons between these mutant strains and their wildtype parent strains initially led to the hypothesis that M35 is necessary for efficient glutamic acid uptake by M. catarrhalis, however this hypothesis was later shown to be incorrect. Efficient uptake of glutamic acid seemed to be mediated by a novel 40 kDa protein that was up-regulated in the deletion mutant strains, presumably to compensate for the lack of M35. M35 was also found to be essential for in vivo survival of M. catarrhalis in the nasal cavities of mice, indicating that it is an essential functional protein for colonisation of the mucosal surface.
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Jonatat, Carola [Verfasser]. "Die Aktivierung des humanen Bronchialepithels durch Moraxella catarrhalis / Carola Jonatat." Berlin : Medizinische Fakultät Charité - Universitätsmedizin Berlin, 2009. http://d-nb.info/1023464616/34.

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Yeo, Siew-Fah. "Epidemiology and antimicrobial resistance of Haemophilus influenzae and Moraxella catarrhalis." Thesis, Queen Mary, University of London, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.309743.

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Books on the topic "Catarrhalis"

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Mirangi, Peter Kiambo. Studies of African malignant catarrhal fever virus and a malignant catarrhal fever-like virus isolated in Minnesota. Birmingham: University of Birmingham, 1991.

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US DEPARTMENT OF AGRICULTURE. Keeping America free from foreign animal diseases. 5. Malignant catarrhal fever. [Washington, D.C.]: U.S. Dept. of Agriculture, 1997.

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Roy, Polly, and Barry M. H. Gorman. Current Topics in Microbiology and Immunology: Bluetongue Viruses. Springer-Verlag Berlin and Heidelberg GmbH & Co. KG, 1990.

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P, Roy, and Gorman B. M, eds. Bluetongue virus. Berlin: Springer-Verlag, 1990.

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ROY, P. Bluetongue Viruses (Current Topics in Microbiology & Immunology). Edited by P. ROY. Springer, 1990.

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Li, Hong. Sheep-associated malignant catarrhal fever: Etiologic and epidemiologic studies. 1994.

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(Editor), P. W. Daniels, Purnomo Ronohardjo (Editor), and Sudarisman (Editor), eds. Malignant Catarrhal Fever in Asian Livestock (Aciar Monograph Series). State Mutual Book & Periodical Service, Ltd., 1988.

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8

White, Arthur. New Self Help: Tinnitus: Self-Help Drug-Free Methods for Dealing with Tinnitus and Catarrhal Deafness (New Self Help). Thorsons, 1986.

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Robinson, Beverley. A Manual on Inhalers, Inhalations and Inhalants; And Guide to Their Discriminating Use in the Treatment of Common Catarrhal Diseases of the Respiratory Tract. Franklin Classics Trade Press, 2018.

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Book chapters on the topic "Catarrhalis"

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Murphy, Timothy F. "Moraxella catarrhalis." In New Bacterial Vaccines, 217–28. Boston, MA: Springer US, 2003. http://dx.doi.org/10.1007/978-1-4615-0053-7_14.

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Ehrhard, Ingrid. "Moraxella catarrhalis." In Lexikon der Infektionskrankheiten des Menschen, 544–47. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-39026-8_708.

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Belkum, Alex van, and Cees M. Verduin. "Moraxella catarrhalis and Kingella kingae." In Principles and Practice of Clinical Bacteriology, 189–204. Chichester, UK: John Wiley & Sons, Ltd, 2006. http://dx.doi.org/10.1002/9780470017968.ch13.

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Aebi, Christoph. "Moraxella catarrhalis – Pathogen or Commensal?" In Advances in Experimental Medicine and Biology, 107–16. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-7185-2_9.

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Doern, Gary V. "Branhamella catarrhalis and Neisseria Species." In Laboratory Diagnosis of Infectious Diseases, 134–42. New York, NY: Springer New York, 1988. http://dx.doi.org/10.1007/978-1-4612-3898-0_13.

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Jacobs, Michael R. "Mechanisms of Resistance in Haemophilus influenzae and Moraxella catarrhalis." In Antimicrobial Drug Resistance, 867–88. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-47266-9_7.

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Jacobs, Michael R. "Mechanisms of Resistance in Haemophilus influenzae and Moraxella catarrhalis." In Antimicrobial Drug Resistance, 783–801. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-60327-595-8_7.

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Olsson-Liljequist, B. "In Vitro Activity of Ciprofloxacin Against Bacteroides, Haemophilus influenzae and Branhamella catarrhalis." In Ciprofloxacin, 33–34. Wiesbaden: Vieweg+Teubner Verlag, 1986. http://dx.doi.org/10.1007/978-3-663-01930-5_9.

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Pollak, Margaret, and John Fry. "Catarrhal children." In Commonsense Paediatrics, 103–11. Dordrecht: Springer Netherlands, 1986. http://dx.doi.org/10.1007/978-94-011-6367-5_13.

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Fry, John. "Catarrhal Children." In Common Diseases, 47–62. Dordrecht: Springer Netherlands, 1985. http://dx.doi.org/10.1007/978-94-009-4924-9_7.

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Conference papers on the topic "Catarrhalis"

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Parameswaran, GI, S. Sethi, and TF Murphy. "Antimicrobial Polypeptides and Moraxella Catarrhalis in COPD." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a3225.

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Ackland, Jodie, Joshua Wallington, David Cleary, Myron Christodoulides, and Karl Staples. "The response of macrophages to Moraxella catarrhalis infection." In ERS International Congress 2017 abstracts. European Respiratory Society, 2017. http://dx.doi.org/10.1183/1393003.congress-2017.pa4127.

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Velkova, Simona, Alina Petris, Dani Lee, Primrose Freestone, Rick Williamson, Soren Beinke, Nikolai Belyaev, et al. "Moraxella catarrhalis infection of healthy and COPD ciliated epithelial cultures." In ERS International Congress 2018 abstracts. European Respiratory Society, 2018. http://dx.doi.org/10.1183/13993003.congress-2018.pa5305.

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Willis, TA, R. Murphy, P. Griffin, E. Frost, S. Ollosson, A. Rogers, S. Carr, et al. "S5 Moraxella catarrhalis attaches to the ciliary tip causing ciliary dyskinesia." In British Thoracic Society Winter Meeting 2018, QEII Centre, Broad Sanctuary, Westminster, London SW1P 3EE, 5 to 7 December 2018, Programme and Abstracts. BMJ Publishing Group Ltd and British Thoracic Society, 2018. http://dx.doi.org/10.1136/thorax-2018-212555.11.

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Parameswaran, GI, S. Sethi, and TF Murphy. "Protease-Antiprotease Balance Is Altered in Colonization and Exacerbation Due to Moraxella Catarrhalis in COPD." In American Thoracic Society 2009 International Conference, May 15-20, 2009 • San Diego, California. American Thoracic Society, 2009. http://dx.doi.org/10.1164/ajrccm-conference.2009.179.1_meetingabstracts.a5659.

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Bertrams, W., C. Rieke, NS Lindhauer, A. Paas, C. Herkt, A. Wesener, K. Hoffmann, A. Vilcinskas, K. Seidel, and B. Schmeck. "Antibacterial activity of a Tribolium castaneum defensin in an in vitro infection model of Moraxella Catarrhalis." In 61. Kongress der Deutschen Gesellschaft für Pneumologie und Beatmungsmedizin e.V. Georg Thieme Verlag KG, 2020. http://dx.doi.org/10.1055/s-0039-3403102.

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Decker, L., P. Mittmann, R. Seidl, and A. Ernst. "Fallbericht: 16-jährige Patientin mit Moraxella catarrhalis-Sepsis mit Halsphlegmone und akuter Pansinusitis bei Metamizol-induzierter Agranulozytose." In Abstract- und Posterband – 91. Jahresversammlung der Deutschen Gesellschaft für HNO-Heilkunde, Kopf- und Hals-Chirurgie e.V., Bonn – Welche Qualität macht den Unterschied. © Georg Thieme Verlag KG, 2020. http://dx.doi.org/10.1055/s-0040-1711536.

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Decker, L., P. Mittmann, R. Seidl, and A. Ernst. "Case report: 16 years old patient with moraxella catarrhalis sepsis with cervical phlegmone and acute pansinusitis in metamizole-induced agranulocytosis." In Abstract- und Posterband – 91. Jahresversammlung der Deutschen Gesellschaft für HNO-Heilkunde, Kopf- und Hals-Chirurgie e.V., Bonn – Welche Qualität macht den Unterschied. © Georg Thieme Verlag KG, 2020. http://dx.doi.org/10.1055/s-0040-1710893.

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Van Damme, Pierre, Geert Leroux-Roels, Corinne Vandermeulen, Iris De Ryck, Annaelisa Tasciotti, Marie Dozot, Luca Moraschini, Marco Testa, and Ashwani Kumar Arora. "Late Breaking Abstract - Safety and immunogenicity of non-typeable H. influenzae (NTHi) and M. catarrhalis (Mcat) adjuvanted vaccines in adults." In ERS International Congress 2018 abstracts. European Respiratory Society, 2018. http://dx.doi.org/10.1183/13993003.congress-2018.pa4088.

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Bertrams, W. "Tribolium Castaneum Defensin 1 Selectively Kills Moraxella Catarrhalis in an In Vitro Infection Model but Does Not Harm Commensal Bacteria." In American Thoracic Society 2021 International Conference, May 14-19, 2021 - San Diego, CA. American Thoracic Society, 2021. http://dx.doi.org/10.1164/ajrccm-conference.2021.203.1_meetingabstracts.a1235.

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You might also be interested in the extended bibliographies on the topic 'Catarrhalis' for particular source types:
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