Sialylation of Neisseria meningitidis lipooligosaccharide inhibits serum bactericidal activity by masking lacto-N-neotetraose
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Inhibitory and bactericidal effects of hydrogen peroxide production by Streptococcus pneumoniae on other inhabitants of the upper respiratory tractTREM-2 binds to lipooligosaccharides of Neisseria gonorrhoeae and is expressed on reproductive tract epithelial cellsInfections of People with Complement Deficiencies and Patients Who Have Undergone SplenectomyThe (alpha2-->8)-linked polysialic acid capsule and lipooligosaccharide structure both contribute to the ability of serogroup B Neisseria meningitidis to resist the bactericidal activity of normal human serum.Update on meningococcal disease with emphasis on pathogenesis and clinical managementProtection by natural human immunoglobulin M antibody to meningococcal serogroup B capsular polysaccharide in the infant rat protection assay is independent of complement-mediated bacterial lysis.Questions about the behaviour of bacterial pathogens in vivo.Structural and immunochemical characterization of the lipooligosaccharides expressed by Neisseria subflava 44Functional activities and immunoglobulin variable regions of human and murine monoclonal antibodies specific for the P1.7 PorA protein loop of Neisseria meningitidisNovel mechanism for the generation of human xeno-autoantibodies against the nonhuman sialic acid N-glycolylneuraminic acid.The interplay between Siglecs and sialylated pathogensThe role of the exopolyphosphatase PPX in avoidance by Neisseria meningitidis of complement-mediated killing.Differential expression and transcriptional analysis of the alpha-2,3-sialyltransferase gene in pathogenic Neisseria sppMeningococcal group W-135 and Y capsular polysaccharides paradoxically enhance activation of the alternative pathway of complement.Neisseria meningitidis: biology, microbiology, and epidemiology.In vivo adaptation and persistence of Neisseria meningitidis within the nasopharyngeal mucosa.Genetic basis for biosynthesis of the (alpha 1-->4)-linked N-acetyl-D-glucosamine 1-phosphate capsule of Neisseria meningitidis serogroup X.α-2,3-sialyltransferase expression level impacts the kinetics of lipooligosaccharide sialylation, complement resistance, and the ability of Neisseria gonorrhoeae to colonize the murine genital tractActivation of toll-like receptor 2 (TLR2) and TLR4/MD2 by Neisseria is independent of capsule and lipooligosaccharide (LOS) sialylation but varies widely among LOS from different strains.Human lipooligosaccharide IGG that prevents endemic meningococcal disease recognizes an internal lacto-N-neotetraose structure.Affinity-purified human immunoglobulin G that binds a lacto-N-neotetraose-dependent lipooligosaccharide structure is bactericidal for serogroup B Neisseria meningitidis.Lipooligosaccharide Structures of Invasive and Carrier Isolates of Neisseria meningitidis Are Correlated with Pathogenicity and CarriageThe relative roles of factor H binding protein, neisserial surface protein A, and lipooligosaccharide sialylation in regulation of the alternative pathway of complement on meningococciAvailable carbon source influences the resistance of Neisseria meningitidis against complement.Effect of host lactate on gonococci and meningococci: new concepts on the role of metabolites in pathogenicity.Meningococcal outer membrane protein NhhA is essential for colonization and disease by preventing phagocytosis and complement attack.Genetically modified L3,7 and L2 lipooligosaccharides from Neisseria meningitidis serogroup B confer a broad cross-bactericidal response.Mechanisms in Neisseria meningitidis for resistance against complement-mediated killing.Low-dose recombinant properdin provides substantial protection against Streptococcus pneumoniae and Neisseria meningitidis infection.Role of lipopolysaccharide sialylation in serum resistance of serogroup B and C meningococcal disease isolates.Influence of the length of the lipooligosaccharide alpha chain on its sialylation in Neisseria meningitidisMannose-binding lectin is present in human semen and modulates cellular adhesion of Neisseria gonorrhoeae in vitro.The sweet side of the pathogenic Neisseria: the role of glycan interactions in colonisation and disease.Chemical synthesis using enzymatically generated building units for construction of the human milk pentasaccharides sialyllacto-N-tetraose and sialyllacto-N-neotetraose epimer.Pro-inflammatory cytokines can act as intracellular modulators of commensal bacterial virulence.Modeling Neisseria meningitidis metabolism: from genome to metabolic fluxes.Progress toward the global control of Neisseria meningitidis: 21st century vaccines, current guidelines, and challenges for future vaccine development.
P2860
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P2860
Sialylation of Neisseria meningitidis lipooligosaccharide inhibits serum bactericidal activity by masking lacto-N-neotetraose
description
1997 nî lūn-bûn
@nan
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
1997年论文
@zh
1997年论文
@zh-cn
name
Sialylation of Neisseria menin ...... by masking lacto-N-neotetraose
@ast
Sialylation of Neisseria menin ...... by masking lacto-N-neotetraose
@en
type
label
Sialylation of Neisseria menin ...... by masking lacto-N-neotetraose
@ast
Sialylation of Neisseria menin ...... by masking lacto-N-neotetraose
@en
prefLabel
Sialylation of Neisseria menin ...... by masking lacto-N-neotetraose
@ast
Sialylation of Neisseria menin ...... by masking lacto-N-neotetraose
@en
P2093
P2860
P1476
Sialylation of Neisseria menin ...... by masking lacto-N-neotetraose
@en
P2093
G A Jarvis
J M Griffiss
M M Estabrook
P2860
P304
P407
P577
1997-11-01T00:00:00Z