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Identification of the integrin binding domain of the Yersinia pseudotuberculosis invasin protein.

Identification of the integrin binding domain of the Yersinia pseudotuberculosis invasin protein. The invasin protein of the pathogenic Yersinia pseudotuberculosis mediates entry of the bacterium into cultured mammalian cells by binding several beta 1 chain integrins. In this study, we identified the region of invasin responsible for cell recognition. Thirty‐two monoclonal antibodies directed against invasin were isolated, and of those, six blocked cell attachment to invasin. These six antibodies recognized epitopes within the last 192 amino acids of invasin. Deletion mutants of invasin and maltose‐binding protein (MBP)‐‐invasin fusion proteins were generated and tested for cell attachment. All of the invasin derivatives that carried the carboxyl‐terminal 192 amino acids retained cell binding activity. One carboxyl‐terminal invasin fragment and seven MBP‐‐invasin fusion proteins were purified. The purified derivatives that retained binding activity inhibited bacterial entry into cultured mammalian cells. These results indicated that the carboxyl‐terminal 192 amino acids of invasin contains the integrin‐binding domain, even though this region does not contain the tripeptide sequence Arg‐Gly‐Asp. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png The EMBO Journal Wiley

Identification of the integrin binding domain of the Yersinia pseudotuberculosis invasin protein.

The EMBO Journal , Volume 9 (6) – Jun 1, 1990

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References (3)

Publisher
Wiley
Copyright
© EMBO
ISSN
0261-4189
eISSN
1460-2075
DOI
10.1002/j.1460-2075.1990.tb08326.x
Publisher site
See Article on Publisher Site

Abstract

The invasin protein of the pathogenic Yersinia pseudotuberculosis mediates entry of the bacterium into cultured mammalian cells by binding several beta 1 chain integrins. In this study, we identified the region of invasin responsible for cell recognition. Thirty‐two monoclonal antibodies directed against invasin were isolated, and of those, six blocked cell attachment to invasin. These six antibodies recognized epitopes within the last 192 amino acids of invasin. Deletion mutants of invasin and maltose‐binding protein (MBP)‐‐invasin fusion proteins were generated and tested for cell attachment. All of the invasin derivatives that carried the carboxyl‐terminal 192 amino acids retained cell binding activity. One carboxyl‐terminal invasin fragment and seven MBP‐‐invasin fusion proteins were purified. The purified derivatives that retained binding activity inhibited bacterial entry into cultured mammalian cells. These results indicated that the carboxyl‐terminal 192 amino acids of invasin contains the integrin‐binding domain, even though this region does not contain the tripeptide sequence Arg‐Gly‐Asp.

Journal

The EMBO JournalWiley

Published: Jun 1, 1990

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