期刊论文详细信息
FEBS Letters
Type 1 M protein of Streptococcus pyogenes
Kopecký, Petr2  Kühnemund, Otto3  Morávek, Ladislav2  Pavlík, Manfred2  Havlíček, Jiří1 
[1] Institute of Hygiene and Epidemiology, Šrobárova 48, 100 42 Prague 10, Czechoslovakia;Institute of Organic Chemistry and Biochemistry, Czechoslovak Academy of Sciences, 166 10 Prague 6, Czechoslovakia;Central Institute of Microbiology and Experimental Therapy, Academy of Sciences of the GDR, Jena, GDR
关键词: (Streptococcus pyogenes) M protein Amino acid sequence Fibrinogen binding Synthetic antigen;   
DOI  :  10.1016/0014-5793(86)81064-X
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

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.

【 授权许可】

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