Listeria monocytogenes Possesses Adhesins for Fibronectin

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Published in:	Infection and Immunity Vol. 67; no. 12; pp. 6698 - 6701
Main Authors:	GILOT, P, ANDRE, P, CONTENT, A. J
Format:	Journal Article
Language:	English
Published:	Washington, DC American Society for Microbiology 01-12-1999 American Society for Microbiology (ASM)
Series:	Note
Subjects:	Adhesins, Bacterial Bacterial Proteins Bacterial Proteins - chemistry Bacterial Proteins - isolation & purification Bacteriology Biological and medical sciences Carrier Proteins Carrier Proteins - chemistry Carrier Proteins - isolation & purification Electrophoresis, Polyacrylamide Gel Fibronectins Fibronectins - metabolism Fundamental and applied biological sciences. Psychology Humans Life Sciences Listeria monocytogenes Listeria monocytogenes - metabolism Microbiology Molecular and Cellular Pathogenesis Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains Specificity Glycoprotein Listeria monocytogenes Bacteria Molecular interaction Host agent relation Adhesin Kinetics Fibronectin
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Abstract	Classifications Services IAI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue IAI About IAI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy Connect to IAI IAI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0019-9567 Online ISSN: 1098-5522 Copyright © 2014 by the American Society for Microbiology. For an alternate route to IAI .asm.org, visit: IAI
AbstractList	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. ABSTRACT 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. 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. Classifications Services IAI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit StumbleUpon Twitter current issue Spotlights in the Current Issue IAI About IAI Subscribers Authors Reviewers Advertisers Inquiries from the Press Permissions & Commercial Reprints ASM Journals Public Access Policy Connect to IAI IAI RSS Feeds 1752 N Street N.W. • Washington DC 20036 202.737.3600 • 202.942.9355 fax • journals@asmusa.org Print ISSN: 0019-9567 Online ISSN: 1098-5522 Copyright © 2014 by the American Society for Microbiology. For an alternate route to IAI .asm.org, visit: IAI ABSTRACT 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.
Author	Jean Content Paul André Philippe Gilot
AuthorAffiliation	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
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Keywords	Specificity Glycoprotein Listeria monocytogenes Bacteria Molecular interaction Host agent relation Adhesin Kinetics Fibronectin
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Snippet	Classifications Services IAI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley Reddit... Listeria monocytogenes is a gram-positive, nonsporulating, food-borne pathogen of humans and animals that is able to invade many eukaryotic cells. Several... ABSTRACT Listeria monocytogenes is a gram-positive, nonsporulating, food-borne pathogen of humans and animals that is able to invade many eukaryotic cells.... ABSTRACT Listeria monocytogenes is a gram-positive, nonsporulating, food-borne pathogen of humans and animals that is able to invade many eukaryotic cells.... Listeria monocytogenes is a gram-positive, nonsporulating, food-borne pathogen of humans and animals that is able to invade many eukaryotic cells. Several...
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SubjectTerms	Adhesins, Bacterial Bacterial Proteins Bacterial Proteins - chemistry Bacterial Proteins - isolation & purification Bacteriology Biological and medical sciences Carrier Proteins Carrier Proteins - chemistry Carrier Proteins - isolation & purification Electrophoresis, Polyacrylamide Gel Fibronectins Fibronectins - metabolism Fundamental and applied biological sciences. Psychology Humans Life Sciences Listeria monocytogenes Listeria monocytogenes - metabolism Microbiology Molecular and Cellular Pathogenesis Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains
Title	Listeria monocytogenes Possesses Adhesins for Fibronectin
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