脆弱拟杆菌中的青霉素结合蛋白

Penicillin-binding proteins in Bacteroides fragilis.

作者信息

Georgopapadakou N H, Smith S A, Sykes R B

出版信息

J Antibiot (Tokyo). 1983 Jul;36(7):907-10. doi: 10.7164/antibiotics.36.907.

DOI:10.7164/antibiotics.36.907

Abstract

The penicillin binding proteins (PBSs) of Bacteroides fragilis, a clinically important Gram-negative rod, were studied. Four PBPs were detected by polyacrylamide gel electrophoresis/fluorography, PBP 4 (molecular weight, 35,000) being a minor PBP. The PBP pattern was thus different from that of the Enterobacteria and Pseudomonads. Antibacterial activity of beta-lactam antibiotics was associated with binding to PBP 1 (molecular weight, 100,000), 2 (molecular weight, 86,000) and 3 (molecular weight, 68,000). Binding to PBP 2 was associated with filamentation while binding to PBP 1 resulted in cell lysis.

摘要

对临床上重要的革兰氏阴性杆菌脆弱拟杆菌的青霉素结合蛋白（PBPs）进行了研究。通过聚丙烯酰胺凝胶电泳/荧光自显影检测到四种PBPs，PBP 4（分子量35,000）是次要的PBP。因此，PBP模式与肠杆菌科细菌和假单胞菌不同。β-内酰胺抗生素的抗菌活性与与PBP 1（分子量100,000）、PBP 2（分子量86,000）和PBP 3（分子量68,000）的结合有关。与PBP 2的结合与丝状化有关，而与PBP 1的结合导致细胞裂解。