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Review

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Bacterial Peptidoglycan-Degrading Enzymes and Their Impact on Host Muropeptide Detection

Humann J.a · Lenz L.L.a, b

Author affiliations

aUniversity of Colorado – Denver and bIntegrated Department of Immunology, National Jewish Health, Denver, Colo., USA

Corresponding Author

Dr. Laurel L. Lenz

National Jewish Health, Integrated Department of Immunology

Rm K510, 1400 Jackson Street

Denver, CO 80206 (USA)

Tel. +1 303 398 1767, Fax +1 303 398 1396, E-Mail lenzl@njc.org

Related Articles for ""

J Innate Immun 2009;1:88–97

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Abstract

Peptidoglycan (PGN) is a major component of the bacterial cell envelope in both Gram-positive and Gram-negative bacteria. These muropeptides can be produced or modified by the activity of bacterial glycolytic and peptidolytic enzymes referred to as PGN hydrolases and autolysins. Some of these bacterial enzymes are crucial for bacterial pathogenicity and have been shown to modulate muropeptide release and/or host innate immune responses. The ability of muropeptides to modulate host responses is due to the fact that eukaryotes do not produce PGN and have instead evolved numerous strategies to detect intact PGN and PGN fragments (muropeptides). Here we review the structure of PGN and introduce the various bacterial enzymes known to degrade or modify bacterial PGN. Host factors involved in PGN and muropeptide detection are also briefly discussed, as are examples of how specific bacterial pathogens use PGN degradation and modification to subvert host innate immunity.

© 2008 S. Karger AG, Basel


Article / Publication Details

First-Page Preview
Abstract of Review

Received: September 17, 2008
Accepted: October 09, 2008
Published online: December 03, 2008
Issue release date: January 2009

Number of Print Pages: 10
Number of Figures: 2
Number of Tables: 0

ISSN: 1662-811X (Print)
eISSN: 1662-8128 (Online)

For additional information: http://www.karger.com/JIN


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