Abstract
In the course of our search for anti-dormant mycobacterial substances from marine organisms, we previously isolated three new aminolipopeptides, named trichoderins A, A1 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.
Original language | English (US) |
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Pages (from-to) | 1287-1290 |
Number of pages | 4 |
Journal | Biological and Pharmaceutical Bulletin |
Volume | 34 |
Issue number | 8 |
DOIs | |
State | Published - Aug 2011 |
Keywords
- ATP synthase
- Aminolipopeptide
- Anti-mycobacterial activity
- Dormant
- Trichoderin A
- Tuberculosis
ASJC Scopus subject areas
- Pharmacology
- Pharmaceutical Science