Cell division protein FtsZ: from structure and mechanism to antibiotic target

被引:47
作者
Silber, Nadine [1 ]
de Opitz, Cruz L. Matos [1 ]
Mayer, Christian [1 ]
Sass, Peter [1 ,2 ]
机构
[1] Univ Tubingen, Interfac Inst Microbiol & Infect Med, Dept Microbial Bioact Cpds, Morgenstelle 28, D-72076 Tubingen, Germany
[2] German Ctr Infect Res DZIF, Partner Site Tubingen, D-72076 Tubingen, Germany
关键词
ADEP; antimicrobials; cytokinesis; divisome; drug discovery; MRSA; PC190723; VRE; Z-RING FORMATION; NUCLEOID OCCLUSION PROTEIN; INHIBITS BACTERIAL PROLIFERATION; SMALL-MOLECULE INHIBITORS; SITE SELECTION SYSTEM; TUBULIN-LIKE PROTEIN; TO-POLE OSCILLATION; EXTREME C-TERMINUS; MIDCELL Z-RING; ESCHERICHIA-COLI;
D O I
10.2217/fmb-2019-0348
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Antimicrobial resistance to virtually all clinically applied antibiotic classes severely limits the available options to treat bacterial infections. Hence, there is an urgent need to develop and evaluate new antibiotics and targets with resistance-breaking properties. Bacterial cell division has emerged as a new antibiotic target pathway to counteract multidrug-resistant pathogens. New approaches in antibiotic discovery and bacterial cell biology helped to identify compounds that either directly interact with the major cell division protein FtsZ, thereby perturbing the function and dynamics of the cell division machinery, or affect the structural integrity of FtsZ by inducing its degradation. The impressive antimicrobial activities and resistance-breaking properties of certain compounds validate the inhibition of bacterial cell division as a promising strategy for antibiotic intervention.
引用
收藏
页码:801 / 831
页数:31
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