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Binding of extracellular matrix laminin to Escherichia coli expressing the Salmonella outer membrane proteins Rck and PagC.

作者信息

Crago A M, Koronakis V

机构信息

Department of Pathology, University of Cambridge, UK.

出版信息

FEMS Microbiol Lett. 1999 Jul 15;176(2):495-501. doi: 10.1111/j.1574-6968.1999.tb13703.x.

DOI:10.1111/j.1574-6968.1999.tb13703.x
PMID:10427733
Abstract

Salmonella Rck and PagC are closely related virulence-associated proteins. When expressed in non-adherent, non-invasive laboratory Escherichia coli, both proteins localised to the outer membrane. Only Rck conferred adhesion to culture cells, but both proteins induced bacterial binding to the cell monolayer background, to extracellular matrix (ECM) preparations, and to the ECM component laminin. Laminin binding was saturable and competitive, and was reduced by removal of carbohydrate side chains. Pre-incubation with laminin targeted recombinant Rck and PagC bacteria directly to the eukaryotic cell surface, and eliminated background binding.

摘要

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