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Infection and Immunity, December 1999, p. 6698-6701, Vol. 67, No. 12
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Listeria monocytogenes Possesses Adhesins for Fibronectin

Philippe Gilot,1,* Paul André,2 and Jean Content1

Department of Virology, Pasteur Institute,1 and Belgian National Reference Center for Listeriosis, Bacteriology Unit, Department of Microbiology, Institute of Hygiene and Epidemiology,2 Brussels, Belgium

Received 29 July 1999/Returned for modification 14 September 1999/Accepted 29 September 1999

Listeria monocytogenes is a gram-positive, nonsporulating, food-borne pathogen of humans and animals that is able to invade many eukaryotic cells. Several listerial surface components have been reported to interact with eukaryotic cell receptors, but the complete mechanism by which the bacteria interact with all of these cell types remains largely unknown. In this work, we found that L. monocytogenes binds to human fibronectin, a 450,000-Da dimeric glycoprotein found in body fluids, on the surface of cells and in an insoluble component of the extracellular matrix. The binding of fibronectin to L. monocytogenes was found to be saturable and dependent on proteinaceous receptors. Five fibronectin-binding proteins of 55.3, 48.6, 46.7, 42.4, and 26.8 kDa were identified. The 55.3-kDa protein was proved to be present at the bacterial cell surface. The binding of L. monocytogenes to fibronectin adds to the number of molecules to which the bacterium is able to adhere and emphasizes the complexity of host-pathogen interactions.

* Corresponding author. Mailing address: Department of Virology, Pasteur Institute, Engeland St. 642, B-1180 Brussels, Belgium. Phone: 32-2-373 34 19. Fax: 32-2-373 32 91. E-mail: pgilot{at}ben.vub.ac.be.

Infection and Immunity, December 1999, p. 6698-6701, Vol. 67, No. 12
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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