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

Journal

JOURNAL OF INNATE IMMUNITY
Volume 1, Issue 2, Pages 88-97

Publisher

KARGER
DOI: 10.1159/000181181

Keywords

Peptidoglycan; Autolysin; Bacteria; Subversion

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Funding

  1. NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI065638] Funding Source: NIH RePORTER
  2. NIAID NIH HHS [R01 AI065638-03, R01 AI065638] Funding Source: Medline

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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. Copyright (C) 2008 S. Karger AG, Basel

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