Development of a microtiter plate fluorescent assay for inhibition studies on the HTLV-1 and HIV-1 proteinases

J Virol Methods. 2004 Aug;119(2):87-93. doi: 10.1016/j.jviromet.2004.03.001.

Abstract

The proteinase of human T-cell leukemia virus type-1 (HTLV-1), similar to the proteinase of human immunodeficiency virus type-1 (HIV-1), is a potential target for chemotherapy, since the virus is associated with a number of human diseases. A microtiter plate fluorescent assay was developed for the HTLV-1 and HIV-1 proteinases for direct comparison of the inhibition profiles of the enzymes. It was established that, except for Indinavir, none of the inhibitors designed against the HIV-1 proteinase were able to inhibit the HTLV-1 proteinase in the studied concentration range, while two reduced peptide bond-containing peptides having the sequence of HTLV-1 cleavage sites were inhibitors of the HTLV-1 proteinase. One of these was potent enough to be used for active site titration of the HTLV-1 proteinase.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Aspartic Acid Endopeptidases / antagonists & inhibitors
  • Aspartic Acid Endopeptidases / chemistry
  • Aspartic Acid Endopeptidases / metabolism*
  • Clinical Enzyme Tests / methods*
  • Fluorescence
  • HIV Protease / chemistry
  • HIV Protease / metabolism*
  • Humans
  • Indinavir / pharmacology
  • Kinetics
  • Peptides / metabolism
  • Substrate Specificity

Substances

  • Peptides
  • Indinavir
  • Aspartic Acid Endopeptidases
  • HIV Protease
  • HTLV-1 protease