Action-mechanism of trichoderin A, an anti-dormant mycobacterial aminolipopeptide from marine sponge-derived Trichoderma sp.

Patamaporn Pruksakorn, Masayoshi Arai, Liu Liu, Prashini Moodley, William Robert Jacobs, Motomasa Kobayashi

Research output: Contribution to journalArticlepeer-review

26 Scopus citations

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 languageEnglish (US)
Pages (from-to)1287-1290
Number of pages4
JournalBiological and Pharmaceutical Bulletin
Volume34
Issue number8
DOIs
StatePublished - Aug 2011

Keywords

  • ATP synthase
  • Aminolipopeptide
  • Anti-mycobacterial activity
  • Dormant
  • Trichoderin A
  • Tuberculosis

ASJC Scopus subject areas

  • Pharmacology
  • Pharmaceutical Science

Fingerprint Dive into the research topics of 'Action-mechanism of trichoderin A, an anti-dormant mycobacterial aminolipopeptide from marine sponge-derived Trichoderma sp.'. Together they form a unique fingerprint.

Cite this