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Infection and Immunity, December 1999, p. 6698-6701, Vol. 67, No. 12
Department of Virology,
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.
0019-9567/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Listeria monocytogenes Possesses
Adhesins for Fibronectin
*
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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