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SpeB modulates fibronectin-dependent internalization of Streptococcus pyogenes by efficient proteolysis of cell-wall-anchored protein F1.

In English

Författare

Summary, in English

SpeB is a cysteine proteinase and virulence determinant secreted by the important human pathogen Streptococcus pyogenes. Recent investigations have suggested a role for SpeB in streptococcal entry into human cells. However, conflicting data concerning the contribution of SpeB to internalization have been presented. Protein F1 is a cell-wall-attached fibronectin (Fn)-binding protein that is present in a majority of streptococcal isolates and is important for internalization. This study shows that protein F1 is efficiently degraded by SpeB, and that removal of protein F1 from the bacterial surface leads to reduced internalization. Whereas M1 protein and protein H, two additional surface proteins of S. pyogenes that bind human plasma proteins, are protected from proteolytic degradation by their ligands, protein F1 is readily cleaved by SpeB also when in complex with Fn. This finding, and the connection between the presence of Fn at the bacterial surface and entry into human cells, suggest that SpeB plays a role in the regulation of the internalization process.

Publiceringsår

2004

Språk

Engelska

Sidor

1559-1569

Publikation/Tidskrift/Serie

Microbiology

Volym

150

Issue

Pt 5

Dokumenttyp

Artikel i tidskrift

Förlag

MAIK Nauka/Interperiodica

Ämne

  • Infectious Medicine

Status

Published

ISBN/ISSN/Övrigt

  • ISSN: 1465-2080