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M proteins are major virulence factors of group A streptococci which enable the bacteria to resist phagocytic attack. Their binding capacity for different plasma proteins seems to be one reason for the antiphagocytic activity of M protein. In the present study we demonstrate that M3 protein, isolated from the streptococcal culture supernatant of strain 4/55, and the recombinant form (rM3), purified from an E. coli lysate after cloning in phage lambda-EMBL3, show a multiple binding to fibrinogen, albumin and fibronectin in Western blot and dot binding assays. Binding of M3 protein to the multifunctional extracellular matrix and plasma protein fibronectin may not only influence phagocytosis but may also contribute to the adherence of these bacteria to endothelial and epithelial cells.
K H Schmidt, and
K Mann, and
J Cooney, and
W Köhler
December 2016,
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K H Schmidt, and
K Mann, and
J Cooney, and
W Köhler
August 1989,
Infection and immunity,
K H Schmidt, and
K Mann, and
J Cooney, and
W Köhler
September 2009,
FASEB journal : official publication of the Federation of American Societies for Experimental Biology,
K H Schmidt, and
K Mann, and
J Cooney, and
W Köhler
June 1985,
Acta pathologica, microbiologica, et immunologica Scandinavica. Section B, Microbiology,
K H Schmidt, and
K Mann, and
J Cooney, and
W Köhler
January 1997,
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K H Schmidt, and
K Mann, and
J Cooney, and
W Köhler
March 1973,
The Journal of infectious diseases,
K H Schmidt, and
K Mann, and
J Cooney, and
W Köhler
August 2016,
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K H Schmidt, and
K Mann, and
J Cooney, and
W Köhler
December 1992,
Infection and immunity,
K H Schmidt, and
K Mann, and
J Cooney, and
W Köhler
December 2000,
Cellular microbiology,
K H Schmidt, and
K Mann, and
J Cooney, and
W Köhler
March 1988,
Zentralblatt fur Bakteriologie, Mikrobiologie, und Hygiene. Series A, Medical microbiology, infectious diseases, virology, parasitology,
