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

Biological and Pharmaceutical Bulletin

Volumn 34, Issue 8, 2011, Pages 1287-1290

  Pruksakorn, Patamaporn ^a   Arai, Masayoshi ^a   Liu, Liu ^a   Moodley, Prashini ^b   Jacobs Jr , William Robert ^c   Kobayashi, Motomasa ^a  

^a OSAKA UNIVERSITY   (Japan)

^b UNIVERSITY OF KWAZULU NATAL   (South Africa)

^c ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

Aminolipopeptide; Anti mycobacterial activity; ATP synthase; Dormant; Trichoderin A; Tuberculosis

Indexed keywords

AMINOLIPOPEPTIDE; ANTIMYCOBACTERIAL AGENT; GENOMIC DNA; POLYPEPTIDE ANTIBIOTIC AGENT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE B; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE H; TRICHODERIN A; UNCLASSIFIED DRUG;

ANTIBIOTIC RESISTANCE; ANTIMICROBIAL ACTIVITY; ARTICLE; ATPB GENE; ATPH GENE; BACTERIAL GENOME; BACTERIUM TRANSFORMATION; CONTROLLED STUDY; COSMID; DNA LIBRARY; DRUG MECHANISM; DRUG SCREENING; DRUG STRUCTURE; ENZYME SYNTHESIS; GENE; GENE IDENTIFICATION; GENE OVEREXPRESSION; GENETIC RESISTANCE; MARINE SPECIES; MYCOBACTERIUM BOVIS; MYCOBACTERIUM SMEGMATIS; NONHUMAN; PROTEIN BINDING; RESTRICTION SITE; TRICHODERMA;

ADENOSINE TRIPHOSPHATE; ANIMALS; ANTI-BACTERIAL AGENTS; BACTERIAL PROTEINS; COSMIDS; DRUG RESISTANCE; GENE LIBRARY; GENOME; LIPOPEPTIDES; MYCOBACTERIUM BOVIS; MYCOBACTERIUM SMEGMATIS; PORIFERA; TRANSFORMATION, GENETIC; TRICHODERMA;

EID: 80051510564     PISSN: 09186158     EISSN: 13475215     Source Type: Journal    
DOI: 10.1248/bpb.34.1287     Document Type: Article

References (18)

1. Idemyor V., J. Natl. Med. Assoc., 99, 1414-1419 (2007).
2. "Global Tuberculosis Control - Epidemiology, Strategy, Financing -, " WHO Report 2009, World Health Organization, 2009. http://www. who.int/tb/publications/global-report/2009/en/index.html
3. Wayne L. G., Hayes L. G., Infect. Immun., 64, 2062-2069 (1996).
4. Lim A., Eleuterio M., Hutter B., Murugasu-Oei B., Dick T., J. Bacteriol., 181, 2252-2256 (1999).
5. Dick T., Lee B. H., Murugasu-Oei B., FEMS Microbiol. Lett., 163, 159-164 (1998).
6. Arai M., Sobou M., Vilchéze C., Baughn A., Hashizume H., Pruksakorn P., Ishida S., Matsumoto M., Jacobs W. R. Jr., Kobayashi M., Bioorg. Med. Chem., 16, 6732-6736 (2008).
7. Arai M., Ishida S., Setiawan A., Kobayashi M., Chem. Pharm. Bull., 57, 1136-1138 (2009).
8. Pruksakorn P., Arai M., Kotoku N., Vilchèze C., Baughn A. D., Moodley P., Jacobs W. R. Jr., Kobayashi M., Bioorg. Med. Chem. Lett., 20, 3658-3663 (2010).
9. Connell N. D., Methods Cell Biol., 45, 107-125 (1994).
10. Balasubramanian V., Pavelka M. S. Jr., Bardarov S. S., Martin J., Weisbrod T. R., McAdam R. A., Bloom B. R., Jacobs W. R. Jr., J. Bacteriol., 178, 273-279 (1996).
11. Banerjee A., Dubnau E., Quemard A., Balasubramanian V., Um K. S., Wilson T., Collins D., de Lisle G., Jacobs W. R. Jr., Science, 263, 227-230 (1994).
12. Telenti A., Philipp W. J., Sreevatsan S., Bernasconi C., Stockbauer K. E., Wieles B., Musser J. M., Jacobs W. R. Jr., Nat. Med., 3, 567-570 (1997).
13. Fukushima K., Arai T., Mori Y., Tsuboi M., Suzuki M., J. Antibiot., 36, 1606-1612 (1983).
14. Fukushima K., Arai T., Mori Y., Tsuboi M., Suzuki M., J. Antibiot., 36, 1613-1630 (1983).
15. Shima A., Fukushima K., Arai T., Terada H., Cell Struct. Funct., 15, 53-58 (1990).
16. Vilchèze C., Wang F., Arai M., Hazbón M. H., Colangeli R., Kremer L., Weisbrod T. R., Alland D., Sacchettini J. C., Jacobs W. R. Jr., Nat. Med., 12, 1027-1029 (2006).
17. Koul A., Dendouga N., Vergauwen K., Molenberghs B., Vranckx L., Willebrords R., Ristic Z., Lill H., Dorange I., Guillemont J., Bald D., Andries K., Nat. Chem. Biol., 3, 323-324 (2007).
18. Koul A., Vranckx L., Dendouga N., Balemans W., Van den Wyngaert I., Vergauwen K., Göhlmann H. W. H., Willebrords R., Poncelet A., Guillemont J., Bald D., Andries K., J. Biol. Chem., 283, 25273-25280 (2008).