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PMID: 3096779 Published · ppublish English Journal Article

Type 1 M protein of Streptococcus pyogenes. N-terminal sequence and peptic fragments.

FEBS letters ·Vol. 208 ·No. 2 ·1986-11-24 ·Pages 435-8

Morávek L, Kühnemund O, Havlícek J, Kopecký P, Pavlík M

Abstract

Limited proteolysis of the surface of type 1 Streptococcus pyogenes by pepsin gives rise to fragment Pep M1 of Mr 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.

MeSH Terms
Amino Acid Sequence Antigens, Bacterial Bacterial Outer Membrane Proteins Bacterial Proteins/classification Carrier Proteins Pepsin A Peptide Fragments/analysis Streptococcus pyogenes/analysis
Chemicals
Antigens, Bacterial Bacterial Outer Membrane Proteins Bacterial Proteins Carrier Proteins Peptide Fragments streptococcal M protein Pepsin A
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Morávek L
Kühnemund O
Havlícek J
Kopecký P
Pavlík M
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
1986-11-24
Pages
435-8
Language
English
Region
England
NLM ID
0155157
Subset
IM
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