Peptidoglycan perception-Sensing bacteria by their common envelope structure

被引:29
作者
Bertsche, Ute [1 ]
Mayer, Christoph [2 ]
Goetz, Friedrich [1 ]
Gust, Andrea A. [3 ]
机构
[1] Univ Tubingen, Interfac Inst Microbiol & Infect Med Tubingen IMI, Microbial Genet, D-72076 Tubingen, Germany
[2] Univ Tubingen, Interfac Inst Microbiol & Infect Med Tubingen IMI, Microbiol Biotechnol, D-72076 Tubingen, Germany
[3] Univ Tubingen, Ctr Plant Mol Biol ZMBP, Plant Biochem, D-72076 Tubingen, Germany
关键词
Peptidoglycan; PAMP; Immune defence; Muropeptide signalling; PGN hydrolases; BETA-LACTAMASE INDUCTION; AUREUS-DERIVED PEPTIDOGLYCAN; GRAM-POSITIVE BACTERIA; INNATE IMMUNE-RESPONSE; ALA-D-ALA; CELL-WALL; RECOGNITION PROTEINS; STAPHYLOCOCCUS-AUREUS; ESCHERICHIA-COLI; CRYSTAL-STRUCTURE;
D O I
10.1016/j.ijmm.2014.12.019
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Most Eubacteria possess peptidoglycan (PGN) or murein that surrounds the cytoplasmic membrane. While on the one hand this PGN sacculus is a very protective shield that provides resistance to the internal turgor and adverse effects of the environment, it serves on the other hand as a major pattern of recognition due to its unique structure. Eukaryotes harness this particular bacterial macromolecule to perceive (pathogenic) microorganisms and initiate their immune defence. PGN fragments are generated by bacteria as turnover products during bacterial cell wall growth and these fragments can be sensed by plants and animals to assess a potential bacterial threat. To increase the sensitivity the concentration of PGN fragments can be amplified by host hydrolytic enzymes such as lysozyine or amidase. But also bacteria themselves are able to perceive information about the state of their cell wall by sensing small soluble fragments released from its PGN, which eventually leads to the induction of antibiotic responses or cell differentiation. How PGN is sensed by bacteria, plants and animals, and how the antibacterial defence is modulated by PGN perception is the issue of this review. (C) 2015 Elsevier GmbH. All rights reserved.
引用
收藏
页码:217 / 223
页数:7
相关论文
共 70 条
[1]   Toll-like receptors in the induction of the innate immune response [J].
Aderem, A ;
Ulevitch, RJ .
NATURE, 2000, 406 (6797) :782-787
[2]   A Peptidoglycan Fragment Triggers β-lactam Resistance in Bacillus licheniformis [J].
Amoroso, Ana ;
Boudet, Julien ;
Berzigotti, Stephanie ;
Duval, Valerie ;
Teller, Nathalie ;
Mengin-Lecreulx, Dominique ;
Luxen, Andre ;
Simorre, Jean-Pierre ;
Joris, Bernard .
PLOS PATHOGENS, 2012, 8 (03)
[3]   Binding and Cellular Activation Studies Reveal That Toll-like Receptor 2 Can Differentially Recognize Peptidoglycan from Gram-positive and Gram-negative Bacteria [J].
Asong, Jinkeng ;
Wolfert, Margreet A. ;
Maiti, Kaustabh K. ;
Miller, Douglas ;
Boons, Geert-Jan .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2009, 284 (13) :8634-8644
[4]   The structure of a LysM domain from E-coli membrane-bound lytic murein transglycosylase D (MltD) [J].
Bateman, A ;
Bycroft, M .
JOURNAL OF MOLECULAR BIOLOGY, 2000, 299 (04) :1113-1119
[5]   Why are pathogenic staphylococci so lysozyme resistant?: The peptidoglycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus [J].
Bera, A ;
Herbert, S ;
Jakob, A ;
Vollmer, W ;
Götz, F .
MOLECULAR MICROBIOLOGY, 2005, 55 (03) :778-787
[6]   Messenger Functions of the Bacterial Cell Wall-derived Muropeptides [J].
Boudreau, Marc A. ;
Fisher, Jed F. ;
Mobashery, Shahriar .
BIOCHEMISTRY, 2012, 51 (14) :2974-2990
[7]   LysM, a widely distributed protein motif for binding to (peptido)glycans [J].
Buist, Girbe ;
Steen, Anton ;
Kok, Jan ;
Kuipers, Oscar R. .
MOLECULAR MICROBIOLOGY, 2008, 68 (04) :838-847
[8]   Lysozymes in the animal kingdom [J].
Callewaert, Lien ;
Michiels, Chris W. .
JOURNAL OF BIOSCIENCES, 2010, 35 (01) :127-160
[9]  
Chamaillard M, 2003, NAT IMMUNOL, V4, P702, DOI 10.1038/ni945
[10]   Host-microbe interactions: Shaping the evolution of the plant immune response [J].
Chisholm, ST ;
Coaker, G ;
Day, B ;
Staskawicz, BJ .
CELL, 2006, 124 (04) :803-814