TAILIEUCHUNG - Báo cáo khoa học: Interactions between M proteins of Streptococcus pyogenes and glycosaminoglycans promote bacterial adhesion to host cells

Several microbial pathogens have been reported to interact with glycosaminoglycans (GAGs) on cell surfaces and in the extracellularmatrix. Herewe demonstrate thatM protein, a major surface-expressed virulence factor of the human bac-terial pathogen, Streptococcus pyogenes, mediates binding to various forms of GAGs. Hence, S. pyogenesstrains expressing a large number of different types of M proteins bound to dermatan sulfate (DS), highly sulfated fractions of heparan sulfate (HS) and heparin, whereas strains deficient in M protein surface expression failed to interact with these GAGs. . | Eur. J. Biochem. 270 2303-2311 2003 FEBS 2003 doi Interactions between M proteins of Streptococcus pyogenes and glycosaminoglycans promote bacterial adhesion to host cells Inga-Maria Frick1 Artur Schmidtchen2 and Ulf Sjobring3 1Department of Cell and Molecular Biology Section for Molecular Pathogenesis department of Medical Microbiology Dermatology and Infection Section for Dermatology and 3Institute of Laboratory Medicine Section for Microbiology Immunology and Glycobiology Lund University Sweden Several microbial pathogens have been reported to interact with glycosaminoglycans GAGs on cell surfaces and in the extracellular matrix. Here we demonstrate that M protein a major surface-expressed virulence factor of the human bacterial pathogen Streptococcus pyogenes mediates binding to various forms of GAGs. Hence S. pyogenes strains expressing a large number of different types of M proteins bound to dermatan sulfate DS highly sulfated fractions of heparan sulfate HS and heparin whereas strains deficient in M protein surface expression failed to interact with these GAGs. Soluble M protein bound DS directly and could also inhibit the interaction between DS and S. pyogenes. Experiments with M protein fragments and with streptococci expressing deletion constructs of M protein showed that determinants located in the NH2-terminalpartaswellas in the C-repeat region of the streptococcal proteins are required for full binding to GAGs. Treatment with ABC-chondroitinase and HS lyase that specifically remove DS and HS chains from cell surfaces resulted in significantly reduced adhesion of S. pyogenes bacteria to human epithelial cells and skin fibroblasts. Together with the finding that exogenous DS and HS could inhibit streptococcal adhesion these data suggest that GAGs function as receptors in M protein-mediated adhesion of S. pyogenes. Keywords Streptococcus pyogenes glycosaminoglycan epithelial cells adhesion. Glycosaminoglycans GAGs belong .

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