MMBR Figure table search 04
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bierne, H.
Right arrow Articles by Cossart, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bierne, H.
Right arrow Articles by Cossart, P.
Microbiology and Molecular Biology Reviews, June 2007, p. 377-397, Vol. 71, No. 2
1092-2172/07/$08.00+0     doi:10.1128/MMBR.00039-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Listeria monocytogenes Surface Proteins: from Genome Predictions to Function

Hélène Bierne* and Pascale Cossart

Institut Pasteur, Unité des Interactions Bactéries Cellules, Paris F-75015, France; INSERM, U604, Paris F-75015, France; and INRA, USC2020, Paris F-75015, France

Summary: The genome of the human food-borne pathogen Listeria monocytogenes is predicted to encode a high number of surface proteins. This abundance likely reflects the ability of this bacterium to survive in diverse environments, including soil, food, and the human host. This review focuses on the various mechanisms by which listerial proteins are attached at the bacterial surface and their many functions, including peptidoglycan metabolism, protein processing, adhesion to host cells, and invasion of host tissues. Extensive in silico analysis of the domains or motifs present in these mosaic proteins reveals that diverse structural features allow the surface proteome to interact with diverse bacterial or host components. This diversity offers new clues about the molecular bases of Listeria pathogenesis.


* Corresponding author. Mailing address: Institut Pasteur, Unité des Interactions Bactéries Cellules, Paris F-75015, France. Phone: 33 1 40 61 31 38. Fax: 33 1 45 68 87 06. E-mail: hbierne{at}pasteur.fr


Microbiology and Molecular Biology Reviews, June 2007, p. 377-397, Vol. 71, No. 2
1092-2172/07/$08.00+0     doi:10.1128/MMBR.00039-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
Appl. Environ. Microbiol. Infect. Immun. Eukaryot. Cell
Mol. Cell. Biol. J. Virol. J. Bacteriol.
ALL ASM JOURNALS

Copyright © 2007 by the American Society for Microbiology. All rights reserved.