Document Detail


An oldie but a goodie - cell wall biosynthesis as antibiotic target pathway.
MedLine Citation:
PMID:  20005776     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Bacterial cell wall biosynthesis represents the target pathway for penicillin, the first antibiotic that was clinically applied on a large scale. Penicillin, by means of its beta-lactam ring, inhibits a number of enzymes which participate in inserting monomeric cell wall building blocks into the cell wall polymer and which have been termed penicillin-binding proteins (PBPs). Ever since the introduction of penicillin, hundreds of beta-lactam antibiotics have been developed and details of their molecular activities elaborated. Meanwhile, various additional classes of antibiotics have been described, which inhibit the same pathway, yet use target molecules others than the PBPs. Such classes include the glycopeptide antibiotics, lipopeptide and lipodepsipeptide antibiotics, the lantibiotics and various other natural product antibiotics with comparatively complex structures. They usually target the membrane-bound steps of the biosynthesis pathway and the highly conserved lipid-bound intermediates of the building block such as lipid II, which represents a particular "Achilles' heel" for antibiotic attack. With in-depth analysis of the activity of more recently identified inhibitors and with the availability of novel techniques for studying prokaryotic cell biology, new insights were obtained into the molecular organisation of the cell wall biosynthesis machinery and its interconnections with other vital cellular processes such as cell division. This, in turn, provides hints for new targets to be exploited and for the development of novel cell wall biosynthesis inhibitors.
Authors:
Tanja Schneider; Hans-Georg Sahl
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review     Date:  2009-12-14
Journal Detail:
Title:  International journal of medical microbiology : IJMM     Volume:  300     ISSN:  1618-0607     ISO Abbreviation:  Int. J. Med. Microbiol.     Publication Date:  2010 Feb 
Date Detail:
Created Date:  2010-02-04     Completed Date:  2010-05-03     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100898849     Medline TA:  Int J Med Microbiol     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  161-9     Citation Subset:  IM    
Copyright Information:
Copyright 2009 Elsevier GmbH. All rights reserved.
Affiliation:
Institute of Medical Microbiology, Immunology and Parasitology-Pharmaceutical Microbiology Section, University of Bonn, Meckenheimer Allee 168, D-53115 Bonn, Germany.
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MeSH Terms
Descriptor/Qualifier:
Animals
Anti-Bacterial Agents / chemistry,  pharmacology*,  therapeutic use
Bacteria* / drug effects,  metabolism
Bacterial Infections / drug therapy*,  microbiology
Biosynthetic Pathways / drug effects*
Cell Wall / drug effects,  metabolism*
Humans
Uridine Diphosphate N-Acetylmuramic Acid / analogs & derivatives,  antagonists & inhibitors
Chemical
Reg. No./Substance:
0/Anti-Bacterial Agents; 0/Uridine Diphosphate N-Acetylmuramic Acid; 0/muramyl-NAc-(pentapeptide)pyrophosphoryl-undecaprenol

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