Interaction of C-terminal sequences of human immunodeficiency virus reverse transcriptase with template primer

J Biol Chem. 1991 Apr 15;266(11):6774-9.

Abstract

We have raised a rabbit monospecific antibody (designated C2003) against a synthetic peptide (CTP66) derived from a conserved sequence in the C-terminal portion of the p66 component of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) (DeVico, A.L., Copeland, T.D., Veronese, F.D., Oroszlan, S., Gallo, R. C., and Sarngadharan, M. G. (1989) AIDS Res. Hum. Retroviruses 5, 51-60). This antibody directly inhibits the polymerase activity of HIV-1 RT and of RTs from a variety of retroviruses. HIV-1 RT is protected from this inhibition by preincubation of the enzyme with template primer prior to treatment with the antibody. Such protection is abrogated when the pretreatment is conducted under conditions of high ionic strength. Kinetic studies showed that the antibody-mediated inhibition is competitive with respect to template primer concentration. These results indicate that C2003 antibody acts to interfere with the template binding function of the enzyme and further indicates that conserved residues recognized by the antibody may be directly involved in this function.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Antigen-Antibody Complex
  • Cell Line
  • Genes, pol*
  • HIV-1 / enzymology*
  • HIV-1 / genetics
  • Humans
  • Immunoglobulin G
  • Kinetics
  • Molecular Sequence Data
  • RNA-Directed DNA Polymerase / genetics
  • RNA-Directed DNA Polymerase / metabolism*
  • Sequence Homology, Nucleic Acid
  • Templates, Genetic

Substances

  • Antigen-Antibody Complex
  • Immunoglobulin G
  • RNA-Directed DNA Polymerase