Journal
BIOLOGICAL & PHARMACEUTICAL BULLETIN
Volume 34, Issue 8, Pages 1287-1290Publisher
PHARMACEUTICAL SOC JAPAN
DOI: 10.1248/bpb.34.1287
Keywords
trichoderin A; ATP synthase; anti-mycobacterial activity; aminolipopeptide; dormant; tuberculosis
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Funding
- Hoansha Foundation
- Uehara Memorial Foundation
- Naito Foundation
- JSPS-South Africa (NRF)
- Ministry of Education, Culture, Sports, Science and Technology of Japan
- Grants-in-Aid for Scientific Research [22659022, 21406002, 21310143, 23102005] Funding Source: KAKEN
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In the course of our search for anti-dormant mycobacterial substances from marine organisms, we previously isolated three new aminolipopeptides, named trichoderins A, M and B, from the culture of the marine sponge-derived fungus of Trichoderma sp. and determined their chemical structures. To identify the gene that could confer a resistance to trichoderin A, we prepared transformants of Mycobacterium (M.) smegmatis, which were transformed with the genomic DNA library of M. bovis BCG constructed in the multi-copy shuttle cosmid pYUB145. Then, the transformant of M. smegmatis, which over-expressed a part of genes that coded mycobacterial ATP synthase, was found to exhibit a resistance to trichoderin A. In addition, trichoderin A reduced ATP contents in M. bovis BCG. These findings elucidated that the anti-mycobacterial activity of trichoderins comes from the inhibition of ATP synthesis.
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