The pH 6 Antigen of Yersinia pestisBinds to β1-Linked Galactosyl Residues in Glycosphingolipids

FGL chaperone-assembled fimbrial polyadhesins: anti-immune armament of Gram-negative bacterial pathogens

“…immunoglobulin G (IgG) and interleukin-1b (IL-1b), involved in the immune system. The binding targets include proteins (Zav'yalov et al, 1995a), glycoproteins (Zav'yalov et al, 1996;Guignot et al, 2000;Anderson et al, 2004a;Berger et al, 2004;Pettigrew et al, 2004;Servin, 2005;Korotkova et al, 2006a, b;Le Bouguénec & Servin, 2006), glycosphingolipids (Payne et al, 1998), phosphatidylcholine and lipoproteins (Makoveichuk et al, 2003). Table 2 describes subunit composition, assembly assisting proteins, species distribution, associated diseases, and receptors for the 23 currently known FGL chaperone-assembled fimbrial polyadhesins.…”

Receptor mimicry as novel therapeutic treatment for biothreat agents

“…GalNAcβ1-4Galβ1-4Glcβ1-1Cer, Galβ1-4Glcβ1-1Cer, collagen, laminin [65][66][67][68] with saccharides, particularly monovalent compounds, may suffer due to degradation by host enzymes under physiological conditions. This could lead to a requirement for excessive and potentially toxic levels to inhibit pathogen attachment.…”

“…Evidence for Y. pestis attachment to oligosaccharides includes reduced attachment to host cells expressing reduced levels of oligosaccharides due to inhibition of carbohydrate biosynthesis by tunicamycin, 39 competitive binding assays 29,39,125 and TLC binding assays. 65,66 The inhibitory effect of anti-adhesion compounds towards Y. pestis attachment to respiratory epithelial and macrophage cell lines has been investigated. 29,39,125 Inhibition of these adhesins in vivo on virulence in pneumonic infection models and their target ligands remain unknown.…”

“…29,39 The GalNAcβ1-4Gal and GalNAcβ1-3Gal moieties are present in asialo-GM1 and asialo-GM2 demonstrated to bind PsaA (pH 6 antigen) of Y. pestis. 65 PsaA forms a fimbrial structure under low pH conditions and mammalian body temperature additionally permitting binding to phosphatidylcholine on A549 cells and surfactant, the lipid moiety of plasma apolipoprotein B and Fc receptors for IgG isotypes. [96][97][98] PsaA-mediated binding to respiratory tract epithelial cells inhibits intracellular uptake, 94 however PsaA is not required for attachment to macrophage cell lines.…”

Significance of glycosphingolipid fatty acid chain length on membrane microdomain‐mediated signal transduction

“…Among the glycosphingolipids, LacCer binds specifically to various pathogenic microorganisms, including Helicobacter pylori, Escherichia coli, Bordetella pertussis, Bacillus dysenteriae, Propionibacterium freudenreichii, and Candida albicans [35][36][37][38][39][40][41][42][43][44][45][46][47][48]. With regard to the interactions between LacCer and microorganisms, thin-layer chromatography and liposome binding assays have indicated that some microorganisms, such as E. coli and H. pylori, bind to the hydroxy fatty acid/sphingosine form but not the non-hydroxy fatty acid/sphingosine form of LacCer [36,38,46,49].…”