Skip to main content
Antimicrobial Agents and Chemotherapy logoLink to Antimicrobial Agents and Chemotherapy
. 1996 Mar;40(3):595–601. doi: 10.1128/aac.40.3.595

Stereospecific reduction of virginiamycin M1 as the virginiamycin resistance pathway in Streptomyces virginiae.

C K Lee 1, M Minami 1, S Sakuda 1, T Nihira 1, Y Yamada 1
PMCID: PMC163164  PMID: 8851577

Abstract

In a cell extract of Streptomyces virginiae, virginiamycin M1 was inactivated in the presence of NADPH, while virginiamycin S remained intact. The inactivated product of virginiamycin M1 was isolated, and structure analysis revealed that the inactivation involves reduction of a C-16 carbonyl group leading to the formation of 16-dihydrovirginiamycin M1. Acetonide and benzylidene acetal derivatives were synthesized from the two hydroxyl groups on C-14 and C-16, and the C-16 stereochemistry was determined by 13C nuclear magnetic resonance spectroscopy. Two methyl groups of the acetonide derivative gave 13C signals of 20.1 and 30.1 ppm, indicating that the relative stereochemistry of the C-14 and C-16 hydroxy groups is syn. Furthermore, irradiation of the benzylidene methine proton gave clear nuclear Overhauser effect enhancement of the C-14 or C-16 methine protons, indicating that H-14 and H-16 were in an axial configuration. From the (14S) absolute configuration of natural virginiamycin M1 and the syn relative configuration for the C-14 and C-16 hydroxyl groups of the inactivated product, the C-16 absolute configuration of the inactivated product was thus identified as R.

Full Text

The Full Text of this article is available as a PDF (234.6 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Cocito C. Antibiotics of the virginiamycin family, inhibitors which contain synergistic components. Microbiol Rev. 1979 Jun;43(2):145–192. doi: 10.1128/mr.43.2.145-192.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. De Meester C., Rondelet J. Microbial acetylation of M factor of virginiamycin. J Antibiot (Tokyo) 1976 Dec;29(12):1297–1305. doi: 10.7164/antibiotics.29.1297. [DOI] [PubMed] [Google Scholar]
  3. Delpierre G. R., Eastwood F. W., Gream G. E., Kingston D. G., Sarin P. S., Todd L., Williams D. H. Antibiotics of the ostreogrycin complex. II. Structure of ostreogrycin A. J Chem Soc Perkin 1. 1966;19:1653–1669. doi: 10.1039/j39660001653. [DOI] [PubMed] [Google Scholar]
  4. Goffic F. L., Capmau M. L., Bonnet D., Cerceau C., Soussy C., Dublanchet A., Duval J. Plasmid-mediated pristinamycin resistance. PAC IIA: a new enzyme which modifies pristinamycin IIA. J Antibiot (Tokyo) 1977 Aug;30(8):665–669. doi: 10.7164/antibiotics.30.665. [DOI] [PubMed] [Google Scholar]
  5. Kim C. H., Otake N., Yonehara H. Studies on mikamycin B lactonase. I. Degradation of mikamycin B by Streptomyces mitakaensis. J Antibiot (Tokyo) 1974 Dec;27(12):903–908. doi: 10.7164/antibiotics.27.903. [DOI] [PubMed] [Google Scholar]
  6. Kim H. S., Nihira T., Tada H., Yanagimoto M., Yamada Y. Identification of binding protein of virginiae butanolide C, an autoregulator in virginiamycin production, from Streptomyces virginiae. J Antibiot (Tokyo) 1989 May;42(5):769–778. doi: 10.7164/antibiotics.42.769. [DOI] [PubMed] [Google Scholar]
  7. Kingston D. G., Todd L., Williams D. H. Antibiotics of the ostreogrycin complex. 3. The structure of ostreogrycin A. Evidence based on nuclear magnetic double resonance experiments and high-resolution mass spectrometry. J Chem Soc Perkin 1. 1966;19:1669–1676. doi: 10.1039/j39660001669. [DOI] [PubMed] [Google Scholar]
  8. Yamada Y., Sugamura K., Kondo K., Yanagimoto M., Okada H. The structure of inducing factors for virginiamycin production in Streptomyces virginiae. J Antibiot (Tokyo) 1987 Apr;40(4):496–504. doi: 10.7164/antibiotics.40.496. [DOI] [PubMed] [Google Scholar]

Articles from Antimicrobial Agents and Chemotherapy are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES