THE CHEMICAL BIOLOGY OF NEW MICROBIAL ANTI-INFECTIVE AGENTS

对三种抗感染药物的作用机制进行了研究。Lariatin A对分枝杆菌具有选择性生长抑制作用。在耻垢分枝杆菌的裂解物中研究了与lariatin A结合的蛋白质，从而鉴定了MSMEG 1878蛋白，其功能尚未报道。Cyslabdan增强了β-内酰胺亚胺培南对耐甲氧西林金黄色葡萄球菌（MRSA）的活性。在MRSA的裂解物中研究了与cyslabdan结合的蛋白质，从而鉴定了SAR 1388，其参与MRSA肽聚糖的五甘氨酸肽间桥的合成。此外，在计算机上研究了葡萄球菌毒素和UPP合成酶的对接模型，以阐明螺环己醛的结合模式。

The mechanism of action of three anti-infective agents was studied. Lariatin A showed selective growth inhibition against mycobacteria. The proteins that bind to lariatin A were investigated in the lysate of Mycobacterium smegmatis, which led to the identification of MSMEG1878 protein whose function has not been reported. Cyslabdan potentiated ss-lactam imipenem activity against methicillin-resistant Staphylococcus aureus(MRSA). The proteins that bind to cyslabdan were investigated in the lysate of MRSA, which led to the identification of SAR1388, which is involved in the synthesis of the pentaglycine interpeptide bridge of the MRSA peptidoglycan. Furthermore, the docking model of viridicatumtoxin and UPP synthase was investigated in silico to elucidate the binding mode of spirohexalines.