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The hemopexin-type repeats of human vitronectin are recognized by Streptococcus pyogenes.

Abstract：

:The specific binding of vitronectin to Streptococcus pyogenes is believed to play an important role in the infection process by mediating adherence of the bacteria to host cells. The domain of vitronectin involved in the interaction with S. pyogenes is unknown. In the present study, we constructed a vitronectin random epitope phage display library, which was used to pan against intact cells of S. pyogenes. Several phage-displayed vitronectin peptides containing a hydrophobic pentapeptide motif within the hemopexin-type repeats were found to bind to streptococci. These data were supported by competition experiments, in which a representative 23-amino acid synthetic vitronectin peptide comprising part of a hemopexin-type repeat inhibited binding of the bacteria to vitronectin, while a control peptide with identical amino acid composition but a scrambled sequence had no effect. Moreover, cells of S. pyogenes were shown to bind to the synthetic peptide as well as to immobilized hemopexin, whose structural homology to the hemopexin-type repeats in the vitronectin molecule has long been underlined. Soluble vitronectin could inhibit streptococcal binding to immobilized hemopexin. These results provide first evidence for a biological role of hemopexin itself and respective repeats in vitronectin in bacterial binding, suggesting that during an infection process these or other hemopexin-type repeat-containing proteins could be potential targets for bacterial attachment and subsequent colonization.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Liang OD,Preissner KT,Chhatwal GS

doi

10.1006/bbrc.1997.6663

subject

Has Abstract

pub_date

1997-05-19 00:00:00

pages

445-9

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(97)96663-8

journal_volume

234

pub_type

杂志文章

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