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Overproduction of the bleomycin‐binding proteins from bleomycin‐producing Streptomyces verticillus and a methicillin‐resistant Staphylococcus aureus in Escherichia coli and their immunological characterisation
Author(s) -
Sugiyama Masanori,
Kumagai Takanori,
Matsuo Hiroaki,
Alam Bhuiyan Zahurul,
Ueda Kazuhiro,
Mochizuki Hiroshi,
Nakamura Norio,
Davies Julian E
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00218-x
Subject(s) - escherichia coli , staphylococcus aureus , bleomycin , monoclonal antibody , microbiology and biotechnology , dna , binding protein , antibody , chemistry , dna binding protein , biology , bacteria , biochemistry , gene , transcription factor , immunology , genetics , chemotherapy
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‐chracterize 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.