Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1992 Dec 15;288(Pt 3):717–719. doi: 10.1042/bj2880717

Observations on the inhibition of HIV-1 reverse transcriptase by catechins.

P S Moore 1, C Pizza 1
PMCID: PMC1131944  PMID: 1281981

Abstract

The sensitivity and specificity of the inhibition of HIV-1 reverse transcriptase by various catechins have been examined. As previously reported, (-)epicatechin 3-gallate inhibits the viral polymerase. However, it is noted here that this inhibition is not observed in the presence of either serum albumin or Triton X-100. Other catechins behave similarly to (-)epicatechin 3-gallate in that they inhibit polymerase activity only in the absence of these reagents. Additionally, other DNA polymerases are inhibited to a similar degree by (-)epicatechin 3-gallate. Taken cumulatively, these results suggest that these catechins, and in particular (-)epicatechin 3-gallate, bind with no apparent selectivity and that the observed inhibition of HIV-1 reverse transcriptase is non-specific in nature.

Full text

PDF
717

Selected References

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

  1. Basu A., Modak M. J. Observations on the suramin-mediated inhibition of cellular and viral DNA polymerases. Biochem Biophys Res Commun. 1985 May 16;128(3):1395–1402. doi: 10.1016/0006-291x(85)91095-2. [DOI] [PubMed] [Google Scholar]
  2. Havsteen B. Flavonoids, a class of natural products of high pharmacological potency. Biochem Pharmacol. 1983 Apr 1;32(7):1141–1148. doi: 10.1016/0006-2952(83)90262-9. [DOI] [PubMed] [Google Scholar]
  3. Hoffman A. D., Banapour B., Levy J. A. Characterization of the AIDS-associated retrovirus reverse transcriptase and optimal conditions for its detection in virions. Virology. 1985 Dec;147(2):326–335. doi: 10.1016/0042-6822(85)90135-7. [DOI] [PubMed] [Google Scholar]
  4. Mitsuya H., Popovic M., Yarchoan R., Matsushita S., Gallo R. C., Broder S. Suramin protection of T cells in vitro against infectivity and cytopathic effect of HTLV-III. Science. 1984 Oct 12;226(4671):172–174. doi: 10.1126/science.6091268. [DOI] [PubMed] [Google Scholar]
  5. Nakane H., Ono K. Differential inhibitory effects of some catechin derivatives on the activities of human immunodeficiency virus reverse transcriptase and cellular deoxyribonucleic and ribonucleic acid polymerases. Biochemistry. 1990 Mar 20;29(11):2841–2845. doi: 10.1021/bi00463a029. [DOI] [PubMed] [Google Scholar]
  6. Nishizawa M., Yamagishi T., Dutschman G. E., Parker W. B., Bodner A. J., Kilkuskie R. E., Cheng Y. C., Lee K. H. Anti-AIDS agents, 1. Isolation and characterization of four new tetragalloylquinic acids as a new class of HIV reverse transcriptase inhibitors from tannic acid. J Nat Prod. 1989 Jul-Aug;52(4):762–768. doi: 10.1021/np50064a016. [DOI] [PubMed] [Google Scholar]
  7. Ono K., Nakane H., Fukushima M., Chermann J. C., Barré-Sinoussi F. Differential inhibitory effects of various flavonoids on the activities of reverse transcriptase and cellular DNA and RNA polymerases. Eur J Biochem. 1990 Jul 5;190(3):469–476. doi: 10.1111/j.1432-1033.1990.tb15597.x. [DOI] [PubMed] [Google Scholar]
  8. Ono K., Nakane H., Fukushima M., Chermann J. C., Barré-Sinoussi F. Inhibition of reverse transcriptase activity by a flavonoid compound, 5,6,7-trihydroxyflavone. Biochem Biophys Res Commun. 1989 May 15;160(3):982–987. doi: 10.1016/s0006-291x(89)80097-x. [DOI] [PubMed] [Google Scholar]
  9. Ono K., Nakane H., Fukushima M. Differential inhibition of various deoxyribonucleic and ribonucleic acid polymerases by suramin. Eur J Biochem. 1988 Mar 1;172(2):349–353. doi: 10.1111/j.1432-1033.1988.tb13893.x. [DOI] [PubMed] [Google Scholar]
  10. TOWN B. W., WILLS E. D., WILSON E. J., WORMALL A. Studies on suramin; the action of the drug on enzymes and some other proteins. General considerations. Biochem J. 1950 Aug;47(2):149–158. doi: 10.1042/bj0470149. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. TOWN B. W., WILLS E. D., WILSON E. J., WORMALL A. Studies on suramin; the action of the drug on enzymes and some other proteins. General considerations. Biochem J. 1950 Aug;47(2):149–158. doi: 10.1042/bj0470149. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES