Relevant bibliographies by topics / Lipooligosaccharide

Academic literature on the topic 'Lipooligosaccharide'

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Published: 4 June 2021

Last updated: 20 February 2023

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Journal articles on the topic "Lipooligosaccharide"

Houliston, R. Scott, Evgeny Vinogradov, Monika Dzieciatkowska, Jianjun Li, Frank St. Michael, Marie-France Karwaski, Denis Brochu, et al. "Lipooligosaccharide ofCampylobacter jejuni." Journal of Biological Chemistry 286, no. 14 (January 21, 2011): 12361–70. http://dx.doi.org/10.1074/jbc.m110.181750.

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Sun, Shuhua, N. Karoline Scheffler, Bradford W. Gibson, Jing Wang, and Robert S. Munson. "Identification and Characterization of the N-Acetylglucosamine Glycosyltransferase Gene of Haemophilus ducreyi." Infection and Immunity 70, no. 10 (October 2002): 5887–92. http://dx.doi.org/10.1128/iai.70.10.5887-5892.2002.

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ABSTRACT Haemophilus ducreyi is the causative agent of chancroid, a sexually transmitted ulcerative disease. In the present study, the Neisseria gonorrhoeae lgtA lipooligosaccharide glycosyltransferase gene was used to identify a homologue in the genome of H. ducreyi. The putative H. ducreyi glycosyltransferase gene (designated lgtA) was cloned and insertionally inactivated, and an isogenic mutant was constructed. Structural studies demonstrated that the lipooligosaccharide isolated from the mutant strain lacked N-acetylglucosamine and distal sugars found in the lipooligosaccharide produced by the parental strain. The isogenic mutant was transformed with a recombinant plasmid containing the putative glycosyltransferase gene. This strain produced the lipooligosaccharide glycoforms produced by the parental strain, confirming that the lgtA gene encodes the N-acetylglucosamine glycosyltransferase.

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Pollard, Angela, Frank St. Michael, Lynn Connor, Wade Nichols, and Andrew Cox. "Structural characterization of Haemophilus parainfluenzae lipooligosaccharide and elucidation of its role in adherence using an outer core mutant." Canadian Journal of Microbiology 54, no. 11 (November 2008): 906–17. http://dx.doi.org/10.1139/w08-082.

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The opportunistic pathogen Haemophilus parainfluenzae is a gram-negative bacterium found in the oropharynx of humans. Haemophilus parainfluenzae is a member of the Pasteurellaceae family in which it is most closely related to Haemophilus sengis and Actinobacillus . Characterization of surface displayed lipooligosaccharide has identified components that are crucial in adherence. We examined the oligosaccharide structure of lipooligosaccharide from 2 clinical isolates of H. parainfluenzae. Core oligosaccharide was isolated by standard methods from purified lipooligosaccharide. Structural information was established by a combination of monosaccharide and methylation analyses, nuclear magnetic resonance spectroscopy, and mass spectrometry revealing the following structures: R-(1-6)-β-Glc-(1-4)-d,d-α-Hep-(1-6)-β-Glc-(1-4)- substituting a tri-heptose-Kdo inner core of L,d-α-Hep-(1-2)-l,d-α-Hep-(1-3)-l,d-α-Hep-(1-5)-α-Kdo at the 4-position of the proximal l,d-α-Hep residue to Kdo, and with a PEtn residue at the 6-position of the central l,d-α-Hep residue. In strain 4282, the R substituent is β-galactose and in strain 4201 there is no substituent at the distal glucose. These analyses have revealed that multiple structural aspects of H. parainfluenzae lipooligosaccharide are comparable with nontypeable Haemophilus influenzae lipooligosaccharide. This study also identified a galactan in strain 4201 and a glucan in strain 4282. Haemophilus parainfluenzae was shown to adhere to a bronchial epithelial cell line to the same degree as nontypeable H. influenzae. However, an H. parainfluenzae mutant lacking the outer core of the lipooligosaccharide showed diminished adherence to the epithelial cells, suggesting that H. parainfluenzae lipooligosaccharide plays a role in tissue colonization.

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Corsaro, M. Michela, Rosa Lanzetta, Ermenegilda Parrilli, Michelangelo Parrilli, M. Luisa Tutino, and Salvatore Ummarino. "Influence of Growth Temperature on Lipid and Phosphate Contents of Surface Polysaccharides from the Antarctic Bacterium Pseudoalteromonas haloplanktis TAC 125." Journal of Bacteriology 186, no. 1 (January 1, 2004): 29–34. http://dx.doi.org/10.1128/jb.186.1.29-34.2004.

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ABSTRACT The chemical structural variations induced by different growth temperatures in the lipooligosaccharide and exopolysaccharide components extracted from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC 125 are described. The increase in phosphorylation with the increase in growth temperature seems to be general, because it happens not only for the lipooligosaccharide but also for the exopolysaccharide. Structural variations in the lipid components of lipid A also occur. In addition, free lipid A is found at both 25 and 4°C but not at 15°C, which is the optimal growth temperature, suggesting a incomplete biosynthesis of the lipooligosaccharide component under the first two temperature conditions.

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Greiner, L. L., H. Watanabe, N. J. Phillips, J. Shao, A. Morgan, A. Zaleski, B. W. Gibson, and M. A. Apicella. "Nontypeable Haemophilus influenzae Strain 2019 Produces a Biofilm Containing N-Acetylneuraminic Acid That May Mimic Sialylated O-Linked Glycans." Infection and Immunity 72, no. 7 (July 2004): 4249–60. http://dx.doi.org/10.1128/iai.72.7.4249-4260.2004.

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ABSTRACT Previous studies suggested that nontypeable Haemophilus influenzae (NTHI) can form biofilms during human and chinchilla middle ear infections. Microscopic analysis of a 5-day biofilm of NTHI strain 2019 grown in a continuous-flow chamber revealed that the biofilm had a diffuse matrix interlaced with multiple water channels. Our studies showed that biofilm production was significantly decreased when a chemically defined medium lacking N-acetylneuraminic acid (sialic acid) was used. Based on these observations, we examined mutations in seven NTHI strain 2019 genes involved in carbohydrate and lipooligosaccharide biosynthesis. NTHI strain 2019 with mutations in the genes encoding CMP-N-acetylneuraminic acid synthetase (siaB), one of the three NTHI sialyltransferases (siaA), and the undecaprenyl-phosphate α-N-acetylglucosaminyltransferase homolog (wecA) produced significantly smaller amounts of biofilm. NTHI strain 2019 with mutations in genes encoding phosphoglucomutase (pgm), UDP-galactose-4-epimerase, and two other NTHI sialyltransferases (lic3A and lsgB) produced biofilms that were equivalent to or larger than the biofilms produced by the parent strain. The biofilm formed by the NTHI strain 2019pgm mutant was studied with Maackia amurensis fluorescein isothiocyanate (FITC)-conjugated and Sambucus nigra tetramethyl rhodamine isocyanate (TRITC)-conjugated lectins. S. nigra TRITC-conjugated lectin bound to this biofilm, while M. amurensis FITC-conjugated lectin did not. S. nigra TRITC-conjugated lectin binding was inhibited by incubation with α2,6-neuraminyllactose and by pretreatment of the biofilm with Vibrio cholerae neuraminidase. Matrix-assisted laser desorption ionization—time of flight mass spectometry analysis of lipooligosaccharides isolated from a biofilm, the planktonic phase, and plate-grown organisms showed that the levels of most sialylated glycoforms were two- to fourfold greater when the lipooligosaccharide was derived from planktonic or biofilm organisms. Our data indicate that NTHI strain 2019 produces a biofilm containing α2,6-linked sialic acid and that the sialic acid content of the lipooligosaccharides increases concomitant with the transition of organisms to a biofilm form.

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Starner, Timothy D., W. Edward Swords, Michael A. Apicella, and Paul B. McCray. "Susceptibility of Nontypeable Haemophilus influenzae to Human β-Defensins Is Influenced by Lipooligosaccharide Acylation." Infection and Immunity 70, no. 9 (September 2002): 5287–89. http://dx.doi.org/10.1128/iai.70.9.5287-5289.2002.

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ABSTRACT Nontypeable Haemophilus influenzae (NTHI) lipooligosaccharide htrB mutants exhibited greater than 45-fold-increased sensitivity to human β-defensin 2 (HBD-2) compared to the wild type. Complementation by htrB in trans to acylation competence reversed this increased sensitivity. In contrast, NTHI was more susceptible to HBD-3 and showed no changes in sensitivity as a result of lipooligosaccharide mutations in oligosaccharide and lipid A biosynthesis genes.

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Lewis, Lisa A., Biswa Choudhury, Jacqueline T. Balthazar, Larry E. Martin, Sanjay Ram, Peter A. Rice, David S. Stephens, Russell Carlson, and William M. Shafer. "Phosphoethanolamine Substitution of Lipid A and Resistance of Neisseria gonorrhoeae to Cationic Antimicrobial Peptides and Complement-Mediated Killing by Normal Human Serum." Infection and Immunity 77, no. 3 (December 29, 2008): 1112–20. http://dx.doi.org/10.1128/iai.01280-08.

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ABSTRACT The capacity of Neisseria gonorrhoeae to cause disseminated gonococcal infection requires that such strains resist the bactericidal action of normal human serum. The bactericidal action of normal human serum against N. gonorrhoeae is mediated by the classical complement pathway through an antibody-dependent mechanism. The mechanism(s) by which certain strains of gonococci resist normal human serum is not fully understood, but alterations in lipooligosaccharide structure can affect such resistance. During an investigation of the biological significance of phosphoethanolamine extensions from lipooligosaccharide, we found that phosphoethanolamine substitutions from the heptose II group of the lipooligosaccharide β-chain did not impact levels of gonococcal (strain FA19) resistance to normal human serum or polymyxin B. However, loss of phosphoethanolamine substitution from the lipid A component of lipooligosaccharide, due to insertional inactivation of lptA, resulted in increased gonococcal susceptibility to polymyxin B, as reported previously for Neisseria meningitidis. In contrast to previous reports with N. meningitidis, loss of phosphoethanolamine attached to lipid A rendered strain FA19 susceptible to complement killing. Serum killing of the lptA mutant occurred through the classical complement pathway. Both serum and polymyxin B resistance as well as phosphoethanolamine decoration of lipid A were restored in the lptA-null mutant by complementation with wild-type lptA. Our results support a role for lipid A phosphoethanolamine substitutions in resistance of this strict human pathogen to innate host defenses.

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Grenier, Daniel. "Binding properties of Treponema denticola lipooligosaccharide." Journal of Oral Microbiology 5, no. 1 (January 1, 2013): 21517. http://dx.doi.org/10.3402/jom.v5i0.21517.

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Arking, Dan, Yanhong Tong, and Daniel C. Stein. "Analysis of Lipooligosaccharide Biosynthesis in theNeisseriaceae." Journal of Bacteriology 183, no. 3 (February 1, 2001): 934–41. http://dx.doi.org/10.1128/jb.183.3.934-941.2001.

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ABSTRACT Neisserial lipooligosaccharide (LOS) contains three oligosaccharide chains, termed the α, β, and γ chains. We used Southern hybridization experiments on DNA isolated from variousNeisseria spp. to determine if strains considered to be nonpathogenic possessed DNA sequences homologous with genes involved in the biosynthesis of these oligosaccharide chains. The presence or absence of specific genes was compared to the LOS profiles expressed by each strain, as characterized by their mobilities on sodium dodecyl sulfate-polyacrylamide gel electrophoresis gel and their reactivities with various LOS-specific monoclonal antibodies. A great deal of heterogeneity was seen with respect to the presence of genes encoding glycosyltransferases in Neisseria. All pathogenic species were found to possess DNA sequences homologous with the lgtgene cluster, a group of genes needed for the synthesis of the α chain. Some of these genes were also found to be present in strains considered to be nonpathogenic, such as Neisseria lactamica, N. subflava, and N. sicca. Some nonpathogenicNeisseria spp. were able to express high-molecular-mass LOS structures, even though they lacked the DNA sequences homologous withrfaF, a gene whose product must act before gonococcal and meningococcal LOS can be elongated. Using a PCR amplification strategy, in combination with DNA sequencing, we demonstrated that N. subflava 44 possessed lgtA, lgtB, andlgtE genes. The predicted amino acid sequence encoded by each of these genes suggested that they encoded functional proteins; however, structural analysis of LOS isolated from this strain indicated that the bulk of its LOS was not modified by these gene products. This suggests the existence of an additional regulatory mechanism that is responsible for the limited expression of these genes in this strain.

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Parker, Craig T., Michel Gilbert, Nobuhiro Yuki, Hubert P. Endtz, and Robert E. Mandrell. "Characterization of Lipooligosaccharide-Biosynthetic Loci of Campylobacter jejuni Reveals New Lipooligosaccharide Classes: Evidence of Mosaic Organizations." Journal of Bacteriology 190, no. 16 (June 13, 2008): 5681–89. http://dx.doi.org/10.1128/jb.00254-08.

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ABSTRACT The lipooligosaccharide (LOS) biosynthesis region is one of the more variable genomic regions between strains of Campylobacter jejuni. Indeed, eight classes of LOS biosynthesis loci have been established previously based on gene content and organization. In this study, we characterize additional classes of LOS biosynthesis loci and analyze various mechanisms that result in changes to LOS structures. To gain further insights into the genomic diversity of C. jejuni LOS biosynthesis region, we sequenced the LOS biosynthesis loci of 15 strains that possessed gene content that was distinct from the eight classes. This analysis identified 11 new classes of LOS loci that exhibited examples of deletions and insertions of genes and cassettes of genes found in other LOS classes or capsular biosynthesis loci leading to mosaic LOS loci. The sequence analysis also revealed both missense mutations leading to “allelic” glycosyltransferases and phase-variable and non-phase-variable gene inactivation by the deletion or insertion of bases. Specifically, we demonstrated that gene inactivation is an important mechanism for altering the LOS structures of strains possessing the same class of LOS biosynthesis locus. Together, these observations suggest that LOS biosynthesis region is a hotspot for genetic exchange and variability, often leading to changes in the LOS produced.

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Dissertations / Theses on the topic "Lipooligosaccharide"

Howard, Michael David. "Antigenic Characterization of Haemophilus somnus Lipooligosaccharide." Thesis, Virginia Tech, 1998. http://hdl.handle.net/10919/35378.

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Lipooligosaccharide (LOS) is the major outer membrane component of many Gram-negative bacteria inhabiting the mucosal membranes, including pathogenic species of Haemophilus and Neisseria. LOS phase variation is one mechanism by which some of these bacteria avoid the host immune response. To better understand LOS phase variation as a virulence mechanism of H. somnus, knowledge of the antigenic diversity of LOS epitopes must be increased. Monoclonal antibodies (MAbs) to H. somnus LOS were produced and used with cross-reacting MAbs to H. aegyptius LOS (MAb 5F5) and Neisseria gonorrhoeae LOS (MAb 3F11) in an ELISA to investigate LOS heterogeneity among forty-five strains of H. somnus. Using three MAbs, thirty-nine of these H. somnus strains were grouped into six antigenic types. Three groups, associated solely with the cross-reacting MAbs 5F5 and 3F11, included the majority (76%) of H. somnus strains. The anti-H. somnus LOS MAb 5D7 recognized a low frequency epitope associated with each of the remaining three groups, which included 11% of the H. somnus strains. Six strains (13%) were not recognized by any of these MAbs.

Inhibition ELISA experiments showed that the MAb 5F5 epitope contained phosphocholine (PCho) and this epitope was present in 56% of the strains tested. The MAb 5F5 epitope is phase variable in H. somnus LOS. How PCho negative variants could allow for systemic infection after initial colonization of the mucosa by PCho positive variants is discussed.

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Tu, Mai H. "Lipooligosaccharide-modified polymeric particles for targeted pulmonary drug delivery." Diss., University of Iowa, 2015. https://ir.uiowa.edu/etd/5666.

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Targeted delivery of drugs directly to the lung epithelium is a promising, though challenging, strategy for the treatment of diseases that affect the lung tissues, such as infections caused by cell-penetrating pathogens, cystic fibrosis, and cancer. With appropriate surface functionality, such as through the attachment of ligands that recognize receptors on cellular surfaces, particulate carriers show improved efficiency in penetrating cells in vitro. A useful class of ligands is produced by many natural human pathogens that infect the respiratory tract. A variety of phylogenetically distinct respiratory bacterial pathogens, such as Haemophilus influenzae, invade host cells in the upper airways by binding of the platelet-activating factor (PAF) receptor via lipooligosaccharide (LOS) glycoforms. By expressing host carbohydrate structures, including phosphorylcholine (ChoP), as a terminal structure on the LOS, the bacteria exhibit molecular mimicry of the host and are able to evade the host immune system. The effectiveness of LOS to induce cellular uptake of the bacteria is dependent on the specific glycoform, with higher ChoP content inducing more bacterial adherance into the lung epithelial. These ligands naturally expressed on bacterial cell surfaces can be isolated and utilized as targeting ligands for delivery vehicles. The studies described in this thesis focus on the development of particulate drug carriers coated with LOS bacterial ligands to enhance the targeting and binding of the carriers to the lung epithelium. Three NTHi clinical isolates were screened to select the strain with the highest ChoP level, and NTHi 3198, an isolate from a patient with chronic obstructive pulmonary disease (COPD), was selected due to its high ChoP activity. LOS from NTHi 3198 was isolated from the bacterial cell membrane, and its activity verified using dot immunoblot and ELISA techniques. Particles (0.2 and 1 µm) composed of polystyrene or poly(lactic-co-glycolic acid) were passively coated with 0.005-50 µg/mL of the isolated LOS 3198 with or without gelatin, coated with gelatin alone, or left uncoated. The LOS coating on the particles was verified using either XPS or ELISA. The association of particles with human bronchial epithelial cells was investigated using two cell culture models, 16HBE14o- and Calu-3, as a function of particle concentration and incubation time. The expression of PAFR on both cells types was confirmed, though the expression of PAFR on 16HBE14o- cells was significantly greater than on Calu-3 cells. Enhancement of 0.2 µm particle-cell association was achieved through coating of the particles with LOS. However, no significant difference in particle-cell association was observed for the 1 µm particles based on particle coating. Control particles of 0.2 µm size, those coated with gelatin (with or without LOS) or uncoated, exhibited low cell binding with a maximum of about 10-18% of cells associated with particles. The ability of the LOS ligand to enhance particle-cell association was coating concentration dependent, with a low coating concentration of LOS having little effect on association, but a concentration 1000-fold higher causing a doubling of the percentage of cells associated with particles at 24 hours. This enhancement was attributed to increased cellular binding of the 0.2 µm particles to the cell surface by confocal microscopy, and was further increased by activating the PAFR prior to incubation with particles. These results suggest the potential application of LOS as a targeting ligand for lung epithelial cells, especially under conditions where PAFR has been activated, such as occurs in lungs infected with Haemophilus influenzae. A significant reduction in particle-cell association was observed when particles were incubated with Calu-3 cells due to the presence of mucus on the cellular surface. This suggests that further optimization of the drug carrier system is needed to efficiently overcome the mucosal fluids.

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Pollard, Angela M. Nichols Wade. "Haemophilus parainfluenzae lipooligosaccharide analysis of structure, toxicity, and role in colonization /." Normal, Ill. : Illinois State University, 2005. http://wwwlib.umi.com/cr/ilstu/fullcit?p3196641.

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Thesis (Ph. D.)--Illinois State University, 2005.
Title from title page screen, viewed September 27, 2006. Dissertation Committee: Wade Nichols (chair), Jon Friesen, Craig Gatto, Laura Vogel, Brian Wilkinson. Includes bibliographical references (leaves 87-93) and abstract. Also available in print.

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O'Connor, Ellen Therese. "What makes a pathogen? genetic and structural heterogeneity of neisserial lipooligosaccharide /." College Park, Md. : University of Maryland, 2006. http://hdl.handle.net/1903/3359.

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Thesis (Ph. D.) -- University of Maryland, College Park, 2006.
Thesis research directed by: Cell Biology & Molecular Genetics. Title from t.p. of PDF. Includes bibliographical references. Published by UMI Dissertation Services, Ann Arbor, Mich. Also available in paper.

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Millar, Lorna Anne. "Diversity and function of the lipooligosaccharide biosynthesis genes from Campylobacter jejuni." Thesis, University of Leicester, 2003. http://hdl.handle.net/2381/30348.

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The enteric pathogen, Campylobacter jejuni, produces a range of LOS structures, however, the precise functions of LOS molecules in infection are largely undetermined. LOS structural diversity is known to arise from variation in LOS biosynthesis gene content and gene sequence. In determining the extent of LOS biosynthesis gene content variation in a group of mainly clinical C. jejuni isolates, in this study two new clusters of LOS biosynthesis genes have been identified. The C. jejuni LOS core can also undergo phase variation due to the presence of GC homopolymeric tracts in the protein coding sequence of biosynthesis genes in the cluster. Therefore, the variation in homopolymeric tract length was investigated in five genes including those in the LOS biosynthesis cluster. Many bacteria are known to vary LPS or LOS structure in response to different environment stimuli. Following the identification of a number of promoters in the LOS core biosynthesis cluster, promoter activity was measured following growth under several different conditions. Although promoter expression did not vary extensively with the different environmental stimuli, less LOS was extracted from cell grown under iron-limitation. The other aim of this work was to investigate LOS biosynthesis gene function. The genes waaF and lpxL are involved in core and lipid A biosynthesis respectively. Mutation of both genes had a substantial effect on LOS core structure and preliminary studies indicate both genes are important for adhesion and invasion of human intestinal cells. The deletion of several genes from the general protein glycosylation pathway also led to the truncation of the LOS core, indicating overlap between the two carbohydrate biosynthesis pathways.

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Chakraborti, Srinjoy. "Therapeutic Antibody Against Neisseria gonorrhoeae Lipooligosaccharide, a Phase-variable Virulence Factor." eScholarship@UMMS, 2017. https://escholarship.umassmed.edu/gsbs_diss/905.

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Neisseria gonorrhoeae (Ng) which causes gonorrhea has become multidrug-resistant, necessitating the development of novel therapeutics and vaccines. mAb 2C7 which targets an epitope within an important virulence factor, the lipooligosaccharide (LOS), is a candidate therapeutic mAb. Ninety-four percent of clinical isolates express the 2C7-epitope which is also a vaccine target. Ng expresses multiple LOS(s) due to phase-variation (pv) of LOS glycosyltransferase (lgt) genes. mAb 2C7 reactivity requires a lactose extension from the LOS core Heptose (Hep) II (i.e. lgtG ‘ON’ [G+]). Pv results in HepI with: two (2-), three (3-), four (4-), or five (5-) hexoses (Hex). How HepI glycans impact Ng infectivity and mAb 2C7 function are unknown and form the bases of this dissertation. Using isogenic mutants, I demonstrate that HepI LOS glycans modulate mAb 2C7 binding. mAb 2C7 causes complement (C’)-dependent bacteriolysis of three (2-Hex/G+, 4-Hex/G+, and 5-Hex/G+) of the HepI mutants in vitro. The 3-Hex/G+ mutant (resistant to C’-dependent bacteriolysis) is killed by neutrophils in the presence of mAb and C’. In mice, 2- and 3-Hex/G+ infections are significantly shorter than 4- and 5-Hex/G+ infections. A chimeric mAb 2C7 that hyperactivates C’, attenuates only 4- and 5-Hex/G+ infections. This study enhances understanding of the role of HepI LOS pv in gonococcal infections and shows that longer HepI glycans are necessary for prolonged infections in vivo. This is the first study that predicts in vitro efficacy of mAb 2C7 against all four targetable HepI glycans thereby strengthening the rationale for development of 2C7-epitope based vaccines and therapeutics.

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Sun, Shuhua. "Cloning and characterization of lipooligosaccharide (LOS) biosynthetic genes of Haemophilus ducreyi /." The Ohio State University, 2001. http://rave.ohiolink.edu/etdc/view?acc_num=osu1488205318509985.

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Chakraborti, Srinjoy. "Therapeutic Antibody Against Neisseria gonorrhoeae Lipooligosaccharide, a Phase-variable Virulence Factor." eScholarship@UMMS, 2005. http://escholarship.umassmed.edu/gsbs_diss/905.

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Phongsisay, Vongsavanh, and vongsavang@yahoo com au. "Campylobacter jejuni and the Guillain-Barré syndrome." RMIT University. Applied Sciences, 2006. http://adt.lib.rmit.edu.au/adt/public/adt-VIT20061221.100446.

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Campylobacter jejuni is an enteric bacterium that causes human gastroenteritis worldwide. Some C. jejuni strains exhibiting human ganglioside-like lipooligosaccharide (LOS) structures, such as GM1 ganglioside, can induce an autoimmune neuropathy of the peripheral nervous system known as the Guillain-Barré syndrome (GBS). This GBS-inducible determinant is encoded by a gene cluster, which shows a high degree of variation among C. jejuni strains. The experiments presented in this thesis were conducted to give a better insight into the LOS synthesis genes in relation to the pathophysiology of C. jejuni. Firstly, a C. jejuni strain without GM1-like molecules was shown to be able to take up large DNA fragments, including LOS synthesis genes, from a strain expressing GM1-like molecules and consequently be transformed into a number of potential GBS-inducible transformants, which exhibited a high degree of genetic and phenotypic diversity. The ability of C. jejuni to take up and integrate foreign DNA explains the genome plasticity observed in this pathogen. Secondly, while attempting to analyse transcription of the LOS gene cluster, neither published methods nor any commercially available kits for RNA isolation could produce DNA-free RNA from C. jejuni. Combinations of these methods were trialled and only the combination of RNAzolB, TURBO DNase treatment, and acid phenol extraction was able to produce DNA-free RNA. The RNA isolated from most C. jejuni strains showed different RNA patterns to that of other bacteria. In addition the RNA from C. jejuni seemed closely associated with DNA compaired to RNA from other organisms. This might be caused by species-specific DNA conformation or chromatin structure. Thirdly, bidirectional transcription was observed in the LOS gene cluster. Both DNA strands were transcribed but transcription of the non-coding strands was at a lower rate, and both sense and antisense transcripts of each LOS gene tested were responsive to acid stress. This unusual transcription might have a potential effect on the expression of the GBS-inducing determinant. Finally, one of the LOS genes, the htrB gene, was further analysed. It was shown that expression of the htrB gene affects morphology, viability, growth ability, and sensitivity to stress environments. These results showed that the LOS molecule of C. jejuni is involved in many processes and is an important molecule for survival.

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Lodge, Karen, and karen lodge@rmit edu au. "A Molecular Investigation of Campylobacter jejuni Pathogenesis." RMIT University. Applied Sciences, 2007. http://adt.lib.rmit.edu.au/adt/public/adt-VIT20080229.151747.

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Campylobacter jejuni is one of the leading bacterial causes of human gastroenteritis world wide and has been linked to several severe complications including autoimmune syndromes which can result in paralysis. Despite being the subject of much study, C. jejuni remains a major public health burden in both developing and developed nations. There is currently no vaccine available for protection against this pathogen and the mechanisms important for C. jejuni pathogenesis are not fully defined. This study has employed a range of experimental approaches to investigate the molecular mechanisms involved in C. jejuni pathogenesis. Lipooligosaccharides (LOSs) are surface structures and known virulence factors of C. jejuni which are involved in serum resistance, resistance to phagocytic killing, endotoxicity and adhesion. Mutagenesis studies targeting the putative LOS biosynthesis genes wlaRF, wlaTA, wlaTB, wlaTC and waaV were performed in order to characterise the proteins encoded by each of these six genes and assess their potential role in C. jejuni pathogenesis in vitro. The gene product of wlaTA was found to be essential for C. jejuni survival and therefore a knock out mutant could not be generated. Phenotypic characterisation of four knock-out mutants confirmed that each gene contributed to the construction of the LOS molecule as all four mutants produced a truncated LOS moiety and altered their immunoreactivity. Further analysis determined that the production of complete LOSs was important for C. jejuni to invade and adhere to both human and chicken cells in vitro. This study identified a link between the inactivation of two LOS biosynthesis genes and the loss of motility, another important virulence factor. A major source of human C. jejuni infection is contact with contaminated poultry. However, C. jejuni exists as a commensal in chickens. It is currently not known why C. jejuni is pathogenic to humans and not to chickens and the differences between these two hosts represent pathogenic and non-pathogenic environments respectively. These environmental differences were exploited in this study. The four conditions investigated were temperature, blood, bile and host cells in vitro. Five different C. jejuni strains (NCTC11168, 81116, HB93-13, a recent human enteritis isolate and a recent chicken isolate) were subjected to modelled

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Books on the topic "Lipooligosaccharide"

Mandrell, Robert Earl. Sialylation of the lipooligosaccharides of neisseria. Birmingham: University of Birmingham, 1992.

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Book chapters on the topic "Lipooligosaccharide"

Christodoulides, Myron. "Preparation of Lipooligosaccharide (LOS) from Neisseria gonorrhoeae." In Neisseria gonorrhoeae, 87–96. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9496-0_6.

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Densen, P., W. D. Zollinger, S. Gulati, and P. A. Rice. "Antibodies against Neisseria gonorrhoeae lipooligosaccharide antigens stimulate neutrophil chemotaxis." In Gonococci and Meningococci, 511–18. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-009-1383-7_80.

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Petrov, A. B., B. F. Semenov, Yu P. Vartanyan, V. P. Torchilin, V. S. Trubetskoy, N. V. Koshkina, B. A. Dmitriev, V. L. L’vov, and I. V. Lopyrev. "Development of Liposomal Vaccine on the Basis of Neisseria meningitidis Lipooligosaccharide." In Neisseriae 1990, edited by Mark Achtman, Peter Kohl, Christian Marchal, Giovanna Morelli, Andrea Seiler, and Burghard Thiesen, 259–64. Berlin, Boston: De Gruyter, 1991. http://dx.doi.org/10.1515/9783110867787-048.

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Apicella, M. A., M. Shero, G. A. Jarvis, J. M. Griffiss, Robert E. Mandrell, and H. Schneider. "Phenotypic variation of the antigen expression of the lipooligosaccharide of Neisseria gonorrhoeae." In Gonococci and Meningococci, 477–83. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-009-1383-7_75.

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Inzana, Thomas J. "The Many Facets of Lipooligosaccharide as a Virulence Factor for Histophilus somni." In Current Topics in Microbiology and Immunology, 131–48. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/82_2015_5020.

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Semenov, B. F., A. B. Petrov, T. A. Chulok, V. P. Torchilin, V. S. Trubetskoy, N. V. Koshkina, V. T. Ivanov, T. M. Andronova, and B. B. Ivanov. "Immunomodulating Complex of Oligopeptide Antigen and Liposomal Form of Neisseria meningitidis Lipooligosaccharide." In Neisseriae 1990, edited by Mark Achtman, Peter Kohl, Christian Marchal, Giovanna Morelli, Andrea Seiler, and Burghard Thiesen, 277–82. Berlin, Boston: De Gruyter, 1991. http://dx.doi.org/10.1515/9783110867787-051.

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Hammack, C. A., J. McLeod Griffiss, M. A. Apicella, and H. Schneider. "Spontaneous variation of lipooligosaccharide components and epitopes in a strain of Neisseria gonorrhoeae." In Gonococci and Meningococci, 537–41. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-009-1383-7_84.

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Kim, J. J., R. E. Mandrell, Hu Zhen, J. T. Poolman, and J. McLeod Griffiss. "Monoclonal antibody identification of shared lipooligosaccharide epitopes of Neisseria meningitidis and Neisseria lactamica." In Gonococci and Meningococci, 563–67. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-009-1383-7_88.

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Stein, Daniel C., and Emanuel F. Petricoin. "Regulation of the addition of 0-side chains on lipooligosaccharide in Neisseria gonorrhoeae." In Neisseriae 1990, edited by Mark Achtman, Peter Kohl, Christian Marchal, Giovanna Morelli, Andrea Seiler, and Burghard Thiesen, 385–90. Berlin, Boston: De Gruyter, 1991. http://dx.doi.org/10.1515/9783110867787-069.

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Dudas, K. C., M. B. Nelson, P. T. LoVerde, and M. A. Apicella. "Pseudomonas pyocin and Neisseria gonorrhoeae: Investigations into the mechanism of gonococcal lipooligosaccharide variant selection." In Neisseriae 1990, edited by Mark Achtman, Peter Kohl, Christian Marchal, Giovanna Morelli, Andrea Seiler, and Burghard Thiesen, 343–48. Berlin, Boston: De Gruyter, 1991. http://dx.doi.org/10.1515/9783110867787-062.

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Conference papers on the topic "Lipooligosaccharide"

Griffiss, Mac. "P678 An effective gonococcal lipooligosaccharide (LOS) vaccine: we know enough to make one." In Abstracts for the STI & HIV World Congress (Joint Meeting of the 23rd ISSTDR and 20th IUSTI), July 14–17, 2019, Vancouver, Canada. BMJ Publishing Group Ltd, 2019. http://dx.doi.org/10.1136/sextrans-2019-sti.744.

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Corrêa, Marilza, Maria Leal, Elza Scott, Adenilza Bello, Eduardo Duarte, and Ellen Jessouroun. "Characterization of native and deacylated Lipid A from lipooligosaccharide of Neisseria meningitidis Serogroup B." In III Seminário Anual Científico e Tecnológico de Bio-Manguinhos. Instituto de Tecnologia em Imunobiológicos, 2015. http://dx.doi.org/10.35259/isi.sact.2015_28598.

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Ishii, Kazuyuki, Yohei Iwasaki, Yasuaki Esumi, and Ryohei Yamasaki. "SYNTHESIS OF A TETRASACCHARIDE, A PARTIAL STRUCTURE OF LIPOOLIGOSACCHARIDE (LOS) PRODUCED BY NEISSERIA GONORRHOEAE STRAIN 15253." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.596.

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Yamasaki, Ryohei, Tetsu Maruyama, Uichirou Yabe, Takuji Aoki, and Shunpei Asuka. "SPECIFIC OLIGOSACCHARIDE STRUCTURE EXPRESSED IN LIPOOLIGOSACCHARIDES ARE IMMUNOGENIC IN HUMANS." In XXIst International Carbohydrate Symposium 2002. TheScientificWorld Ltd, 2002. http://dx.doi.org/10.1100/tsw.2002.706.

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