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Oxford University Press, FEMS Microbiology Letters, 2(176), p. 495-501, 1999

DOI: 10.1111/j.1574-6968.1999.tb13703.x

Oxford University Press (OUP), FEMS Microbiology Letters, 2(176), p. 495-501

DOI: 10.1016/s0378-1097(99)00279-7

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Binding of extracellular matrix laminin toEscherichia coliexpressing theSalmonellaouter membrane proteins Rck and PagC

Journal article published in 1999 by Aimee M. Crago, Vassilis Koronakis ORCID
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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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.