Meningococcal lipopolysaccharide (LPS) is of crucial importance for the pathogenesis of invasive infection. We show that sialylation and elongation of the alpha-chain effectively shields viable unencapsulated Neisseria meningitidis from recognition by human dendritic cells (DC). In contrast, beta- and gamma- chain of the LPS carbohydrate moiety play only a minor role in the interaction with DC. The protective function of the LPS for the bacteria can be counteracted in vivo by phase variation of the lgtA gene encoding LPS glycosyltransferase A. Capsule expression protects N. meningitidis efficiently from recognition and phagocytosis by DC independent of the LPS structure. Despite the significant impact of LPS composition on the adhesion and phagocytosis of N. meningitidis no differences were found in terms of cytokine levels secreted by DC for IL1-beta, IL-6, IL-8, TNF-alpha, IFN-gamma and GM-CSF. However, significantly lower levels of the regulatory mediator IL-10 were induced by encapsulated strains in comparison to isogenic unencapsulated derivatives. IL-10 secretion was shown to depend on phagocytosis because poly alpha-2,8 sialic acid did not influence IL-10 secretion. The use of truncated LPS isoforms in vaccine preparations can therefore not only result in attenuation but also in more efficient targeting of DC.
%0 Journal Article
%1 kurzai_carbohydrate_2005
%A Kurzai, Oliver
%A Schmitt, Corinna
%A Claus, Heike
%A Vogel, Ulrich
%A Frosch, Matthias
%A Kolb-Mäurer, Annette
%D 2005
%J Cellular Microbiology
%K A B, Bacterial Capsules, Cells, Class Cultured, Cytokines, Dendritic Electron, Glycosyltransferases, Humans, Lipopolysaccharides, Membrane Microscopy, Mutation, Neisseria Outer Phagocytosis, Proteins, Receptors, Scavenger Serogroup Transmission, ag_kurzai meningitidis, {N-Acetylglucosaminyltransferases,}
%N 9
%P 1319--1334
%R 10.1111/j.1462-5822.2005.00559.x
%T Carbohydrate composition of meningococcal lipopolysaccharide modulates the interaction of Neisseria meningitidis with human dendritic cells
%U http://www.ncbi.nlm.nih.gov/pubmed/16098219
%V 7
%X Meningococcal lipopolysaccharide (LPS) is of crucial importance for the pathogenesis of invasive infection. We show that sialylation and elongation of the alpha-chain effectively shields viable unencapsulated Neisseria meningitidis from recognition by human dendritic cells (DC). In contrast, beta- and gamma- chain of the LPS carbohydrate moiety play only a minor role in the interaction with DC. The protective function of the LPS for the bacteria can be counteracted in vivo by phase variation of the lgtA gene encoding LPS glycosyltransferase A. Capsule expression protects N. meningitidis efficiently from recognition and phagocytosis by DC independent of the LPS structure. Despite the significant impact of LPS composition on the adhesion and phagocytosis of N. meningitidis no differences were found in terms of cytokine levels secreted by DC for IL1-beta, IL-6, IL-8, TNF-alpha, IFN-gamma and GM-CSF. However, significantly lower levels of the regulatory mediator IL-10 were induced by encapsulated strains in comparison to isogenic unencapsulated derivatives. IL-10 secretion was shown to depend on phagocytosis because poly alpha-2,8 sialic acid did not influence IL-10 secretion. The use of truncated LPS isoforms in vaccine preparations can therefore not only result in attenuation but also in more efficient targeting of DC.
@article{kurzai_carbohydrate_2005,
abstract = {Meningococcal lipopolysaccharide {(LPS)} is of crucial importance for the pathogenesis of invasive infection. We show that sialylation and elongation of the alpha-chain effectively shields viable unencapsulated Neisseria meningitidis from recognition by human dendritic cells {(DC).} In contrast, beta- and gamma- chain of the {LPS} carbohydrate moiety play only a minor role in the interaction with {DC.} The protective function of the {LPS} for the bacteria can be counteracted in vivo by phase variation of the {lgtA} gene encoding {LPS} glycosyltransferase A. Capsule expression protects N. meningitidis efficiently from recognition and phagocytosis by {DC} independent of the {LPS} structure. Despite the significant impact of {LPS} composition on the adhesion and phagocytosis of N. meningitidis no differences were found in terms of cytokine levels secreted by {DC} for {IL1-beta,} {IL-6,} {IL-8,} {TNF-alpha,} {IFN-gamma} and {GM-CSF.} However, significantly lower levels of the regulatory mediator {IL-10} were induced by encapsulated strains in comparison to isogenic unencapsulated derivatives. {IL-10} secretion was shown to depend on phagocytosis because poly alpha-2,8 sialic acid did not influence {IL-10} secretion. The use of truncated {LPS} isoforms in vaccine preparations can therefore not only result in attenuation but also in more efficient targeting of {DC.}},
added-at = {2011-04-07T15:44:20.000+0200},
author = {Kurzai, Oliver and Schmitt, Corinna and Claus, Heike and Vogel, Ulrich and Frosch, Matthias and {Kolb-Mäurer}, Annette},
biburl = {https://www.bibsonomy.org/bibtex/28e1c613209dd7bef8c7780658e6dddba/hymi},
doi = {10.1111/j.1462-5822.2005.00559.x},
interhash = {f285bd6552fe1cdd6854e20120ff8f45},
intrahash = {8e1c613209dd7bef8c7780658e6dddba},
issn = {1462-5814},
journal = {Cellular Microbiology},
keywords = {A B, Bacterial Capsules, Cells, Class Cultured, Cytokines, Dendritic Electron, Glycosyltransferases, Humans, Lipopolysaccharides, Membrane Microscopy, Mutation, Neisseria Outer Phagocytosis, Proteins, Receptors, Scavenger Serogroup Transmission, ag_kurzai meningitidis, {N-Acetylglucosaminyltransferases,}},
month = sep,
note = {{PMID:} 16098219},
number = 9,
pages = {1319--1334},
timestamp = {2011-04-07T16:41:09.000+0200},
title = {Carbohydrate composition of meningococcal lipopolysaccharide modulates the interaction of Neisseria meningitidis with human dendritic cells},
url = {http://www.ncbi.nlm.nih.gov/pubmed/16098219},
volume = 7,
year = 2005
}