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Type 1 M protein of Streptococcus pyogenes
Author(s) -
Morávek Ladislav,
Kühnemund Otto,
Havlíček Jiří,
Kopecký Petr,
Pavlík Manfred
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)81064-x
Subject(s) - streptococcus pyogenes , proteolysis , virulence , peptide sequence , homology (biology) , pepsin , biology , chemistry , biochemistry , fibrinogen , amino acid , microbiology and biotechnology , genetics , bacteria , gene , enzyme , staphylococcus aureus
Limited proteolysis of the surface of type 1 Streptococcus pyogenes by pepsin gives rise to fragment Pep M1 of M r 20270 as the main product which covers the N‐terminal part of the M protein. The amino acid sequence was determined of the N‐terminal region of the M protein representing the most exposed part of the molecule on the surface fibrils of streptococcal cells, which seems to be very important for the differentiation of the individual serological types. The sequence differs from the homologous N‐terminal sequences of types 5, 6 and 24, and shows a homology with sequences repeating in the chain of type 24. Fragment Pep M1 binds to fibrinogen; the absence of its 30 N‐terminal amino acid residues, however, abolishes this interaction which is believed to play a role in the virulence of S. pyogenes .