Recruitment of penicillin-binding protein PBP2 to the division site of Staphylococcus aureus is dependent on its transpeptidation substrates
Recruitment of penicillin-binding protein PBP2 to the division site of Staphylococcus aureus is dependent on its transpeptidation substrates
复制标题
DOI：
10.1111/j.1365-2958.2004.04420.x
复制
发表时间：
2005-02-01
影响因子：
3.6
通讯作者：
Errington, J
中科院分区：
文献类型：
--
作者：
Pinho, MG;Errington, J
金黄色葡萄球菌青霉素结合蛋白PBP 2是参与肽聚糖组装的最后阶段的酶，并且在该病原体的甲氧西林耐药机制中起重要作用。PBP 2定位于分裂位点，但苯唑西林酰化后阻止其向形成分裂隔膜的募集。抗生素的存在不影响FtsZ环的维护，也不影响外部化肽聚糖前体的定位。当PBP 2的五肽底物通过加入D-环丝氨酸消除或通过加入万古霉素阻断时，也观察到PBP 2的离域。综上所述，这些观察结果表明，PBP 2通过结合其底物被募集到分裂位点，该底物位于该位置。在耐甲氧西林的S.在金黄色葡萄球菌中，苯唑西林的加入不导致PBP 2的离域，表明酰化的PBP 2可以通过功能性PBP 2A（该抗性机制的中心元件）保持在适当位置。
Staphylococcus aureus penicillin-binding protein PBP2 is an enzyme involved in the last stages of peptidoglycan assembly and is an important player in the mechanism of methicillin resistance of this pathogen. PBP2 localized to the division site but its recruitment to the forming division septum was prevented after acylation by oxacillin. The presence of the antibiotic did not affect FtsZ ring maintenance nor the localization of externalized peptidoglycan precursors. Delocalization of PBP2 was also observed when its pentapeptide substrate was eliminated by addition of D-cycloserine or blocked by addition of vancomycin. Taken together these observations suggest that PBP2 is recruited to the division site by binding to its substrate, which is localized at that place. In methicillin-resistant S. aureus, addition of oxacillin does not result in delocalization of PBP2 indicating that acylated PBP2 can be maintained in place by functional PBP2A, the central element of this resistance mechanism.