Literature DB >> 8330904

Lipo-oligosaccharides (LOS) of mucosal pathogens: molecular mimicry and host-modification of LOS.

R E Mandrell1, M A Apicella.   

Abstract

Immunochemical studies of the lipo-oligosaccharides (LOS) of the Gram-negative bacteria Neisseria gonorrhoeae and Neisseria meningitidis have revealed some interesting structural characteristics of these LOS that might relate to their roles during pathogenesis. The carbohydrate moieties of the LOS of pathogenic Neisseria mimic carbohydrates present in glycosphingolipids of human cells. Firstly, an LOS component present among a number of Neisseria species is antigenically and/or chemically identical to lactoneoseries glycosphingolipids present in human cells. The lactoneoseries LOS becomes sialylated on Neisseria gonorrhoeae when they are grown in the presence of cytidine 5'-monophospho-N-acetyl-neuraminic acid (CMP-NANA), the nucleotide sugar for sialic acid. Examination of gonococci present in exudates from males with natural infection indicates that sialylation also occurs in vivo. The mechanism for this process apparently involves a bacterial sialyltransferase scavenging available host CMP-NANA ("host-modification" of LOS) and transferring the sialic acid to the lactoneoserieslike LOS. Strains of N. meningitidis and Haemophilus influenzae also express similarly sialylated LOS suggesting that this is a common mechanism of pathogenesis among these bacteria. Additional examples of LOS that mimic other glycosphingolipid series have been identified also and the fact that multiple series can be expressed in a single population of gonococci suggests that a diverse set of LOS can be presented to the host during infection. It is possible that this diverse set of LOS serve different functions for the bacteria in various hosts and/or environments during infection.

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Year:  1993        PMID: 8330904     DOI: 10.1016/S0171-2985(11)80352-9

Source DB:  PubMed          Journal:  Immunobiology        ISSN: 0171-2985            Impact factor:   3.144


  62 in total

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3.  The relative roles of factor H binding protein, neisserial surface protein A, and lipooligosaccharide sialylation in regulation of the alternative pathway of complement on meningococci.

Authors:  Lisa A Lewis; Matthew Carter; Sanjay Ram
Journal:  J Immunol       Date:  2012-04-13       Impact factor: 5.422

Review 4.  Virulence determinants involved in differential host niche adaptation of Neisseria meningitidis and Neisseria gonorrhoeae.

Authors:  Stephanie Schielke; Matthias Frosch; Oliver Kurzai
Journal:  Med Microbiol Immunol       Date:  2010-04-09       Impact factor: 3.402

5.  Serum antibodies against gangliosides and Campylobacter jejuni lipopolysaccharides in Miller Fisher syndrome.

Authors:  A Neisser; H Bernheimer; T Berger; A P Moran; B Schwerer
Journal:  Infect Immun       Date:  1997-10       Impact factor: 3.441

6.  Differential expression and transcriptional analysis of the alpha-2,3-sialyltransferase gene in pathogenic Neisseria spp.

Authors:  Mathanraj Packiam; Dawn M Shell; Shi V Liu; Yao-Bin Liu; David J McGee; Ranjana Srivastava; Samar Seal; Richard F Rest
Journal:  Infect Immun       Date:  2006-05       Impact factor: 3.441

7.  Structure and mechanism of the lipooligosaccharide sialyltransferase from Neisseria meningitidis.

Authors:  Leo Y-C Lin; Bojana Rakic; Cecilia P C Chiu; Emilie Lameignere; Warren W Wakarchuk; Stephen G Withers; Natalie C J Strynadka
Journal:  J Biol Chem       Date:  2011-08-31       Impact factor: 5.157

8.  Sialylation of lipooligosaccharides promotes biofilm formation by nontypeable Haemophilus influenzae.

Authors:  W Edward Swords; Miranda L Moore; Luciana Godzicki; Gail Bukofzer; Michael J Mitten; Jessica VonCannon
Journal:  Infect Immun       Date:  2004-01       Impact factor: 3.441

Review 9.  The molecular mechanisms used by Neisseria gonorrhoeae to initiate infection differ between men and women.

Authors:  Jennifer L Edwards; Michael A Apicella
Journal:  Clin Microbiol Rev       Date:  2004-10       Impact factor: 26.132

10.  Identification of the gonococcal glmU gene encoding the enzyme N-acetylglucosamine 1-phosphate uridyltransferase involved in the synthesis of UDP-GlcNAc.

Authors:  J Ullrich; J P van Putten
Journal:  J Bacteriol       Date:  1995-12       Impact factor: 3.490

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