A novel, anchorless streptococcal surface protein that binds to human immunoglobulins.

Abstract:

:We have characterized a novel surface protein from urea extract of whole cells of group A Streptococcus pyogenes (GAS). A major protein band (35kD) was found to hybridize with human IgG by Western blotting. A search of the N-terminal amino acid sequence of this protein by using the GAS genome sequence database revealed an open reading frame that encoded a 38-kDa protein with a signal peptide sequence. We have named this protein streptococcal immunoglobulin-binding protein 35 (Sib35). It was found to be an anchorless protein with no LPXTG motif, distinct from the M protein superfamily exhibiting immunoglobulin-binding activity, and partially secreted in the culture supernatant. Recombinant Sib35 was also shown to bind human IgA and IgM. The sib35 gene was found in all GAS strains examined, but not in oral, group B, C, or G streptococcal strains. These results suggest that Sib35 is a unique immunoglobulin-binding protein in GAS.

authors

Kawabata S,Tamura Y,Murakami J,Terao Y,Nakagawa I,Hamada S

doi

10.1016/s0006-291x(02)02078-8

subject

Has Abstract

pub_date

2002-09-06 00:00:00

pages

1329-33

issue

5

eissn

0006-291X

issn

1090-2104

pii

S0006291X02020788

journal_volume

296

pub_type

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