Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.1.53 (sialidase)
 2,694 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The adherence of the human respiratory pathogen, Bordetella pertussis, to purified glycosphingolipids was investigated using thin layer chromatography overlay assays. Both virulent and avirulent strains of B. pertussis bound to asialo GM1. The bacterium did not bind to the gangliosides GM1, GD1a, GD1b, and GT1b, nor to lactosylceramide, trihexosylceramide, globoside, or Forssman antigen. However, after treatment of the chromatography plates with sialidase, B. pertussis bound to the gangliosides GM1, GM2, GD1a, GD1b, and GT1b but not to GM3. Comparison of the oligosaccharide structures of these gangliosides suggests that the minimum sugar structure needed for avid bacterial binding is GalNAc beta 4Gal. This structure has been previously implicated as a receptor for other human respiratory pathogens (Krivan, H. C., Roberts, D. D., Ginsburg, V. (1988) Proc. Natl. Acad. Sci. U.S.A 85, 6157-6161). Virulent strains of B. pertussis also bound specifically to sulfatide. This response was dose-dependent and inhibited by the anionic polysaccharide dextran sulfate. The sulfated-sugars dextran sulfate, fucoidan, and heparin inhibited the attachment of virulent strains of B. pertussis to human WiDr cells and to hamster trachea cells indicating that sulfatides on the surface of mammalian cells may function as a receptor for B. pertussis. The occurrence of both sulfatides and asialo GM1 in human lung and trachea suggests that these glycolipids may serve as specific receptors for B. pertussis.
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PMID:Adhesion of Bordetella pertussis to sulfatides and to the GalNAc beta 4Gal sequence found in glycosphingolipids. 191 2

Tex was originally identified in Bordetella pertussis, where it serves as a transcriptional regulator of toxin genes. However, the Tex of Streptococcus pneumoniae has no regulatory function in the expression of the pneumococcal major toxin pneumolysin. Here, we identified the CPE2168 gene as Tex in Clostridium perfringens, and examined the roles of Tex in toxin gene expression. We found that the deletion mutant for Tex does not affect growth, but the mRNA levels of three hyaluronidase genes (nagH, nagJ, and nagL) and an exo-sialidase (nanJ) were reduced to less than 50% as compared to the parent strain, C. perfringens strain 13. On the other hand, Tex did not affect the expression of proteases, enterotoxins, hemolysins, either of two hyaluronidase genes (nagI and nagK), an exo-sialidase (nanI), or adhesins. Moreover, purified Tex bound to the 5'-portion of target gene mRNAs. Based on these results, we propose that Tex positively regulates the gene expression of a set of toxin genes in C. perfringens.
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PMID:Effects of depletion of RNA-binding protein Tex on the expression of toxin genes in Clostridium perfringens. 2069 86