Sugiyama M, Kumagai T, Matsuo H, Bhuiyan M Z, Ueda K, Mochizuki H, Nakamura N, Davies J E
Institute of Pharmaceutical Sciences, Hiroshima University School of Medicine, Japan.
FEBS Lett. 1995 Mar 27;362(1):80-4. doi: 10.1016/0014-5793(95)00218-x.
The bleomycin-binding proteins designated BLMA and BLMS, which confer resistance to bleomycin (Bm), from Bm-producing Streptomyces verticillus ATCC15003 and a methicillin-resistant Staphylococcus aureus B-26, respectively, were overexpressed in Escherichia coli. The present study showed that both BLMA and BLMS quench the antibacterial activity of Bm by the binding to the drug. To immuno-characterize the Bm-binding proteins, we constructed a monoclonal antibody against BLMA. The antibody, designated 893-12, did not cross react to BLMS and another Bm-binding protein from tallysomycin-producing Streptoalloteichus hindustanus. Although the ability of Bm to cleavage DNA was eliminated by a binding of BLMA to Bm, as shown by Sugiyama et al. [Gene 151 (1994) 11-15], the Bm-induced DNA degradation was restored by pre-incubation of BLMA with the anti-BLMA monoclonal antibody.
分别来自产博来霉素的轮状链霉菌ATCC15003和耐甲氧西林金黄色葡萄球菌B-26的赋予对博来霉素（Bm）抗性的博来霉素结合蛋白BLMA和BLMS在大肠杆菌中过表达。本研究表明，BLMA和BLMS均通过与药物结合来淬灭Bm的抗菌活性。为了对Bm结合蛋白进行免疫特性分析，我们构建了一种针对BLMA的单克隆抗体。该抗体命名为893-12，与BLMS以及来自产 tallysomycin的印度链霉菌的另一种Bm结合蛋白无交叉反应。尽管如杉山等人[《基因》151(1994)11 - 15]所示，BLMA与Bm结合消除了Bm切割DNA的能力，但通过将BLMA与抗BLMA单克隆抗体预孵育，Bm诱导的DNA降解得以恢复。
