Identification of an amino acid substitution involved in the reduction of sensitivity of HIV-1 to an inhibitor of viral proteinase

O Turriziani; G Antonelli; H Jacobsen; J Mous; E Riva; M Pistello; F Dianzani

Identification of an amino acid substitution involved in the reduction of sensitivity of HIV-1 to an inhibitor of viral proteinase

Acta Virol. 1994 Oct;38(5):297-8.

Authors

O Turriziani¹, G Antonelli, H Jacobsen, J Mous, E Riva, M Pistello, F Dianzani

Affiliation

¹ Institute of Virology, University La Sapienza, Rome, Italy.

PMID: 7726006

Abstract

Clones derived from HIV variants previously characterized as resistant to Ro31-8959, an inhibitor of viral proteinase (PR), were sequenced. Substitution of glycine by valine at position 48 of the PR protein was found. None of the 20 clones derived from wild type HTLV-IIIB contain this mutation. Since such a position is located in a conserved region of PR, it is possible that the substitution can affect the interaction of the enzyme with the inhibitor.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Base Sequence
DNA Primers
Drug Resistance, Microbial / genetics
Glycine / genetics
HIV / genetics
HIV / metabolism
HIV Protease Inhibitors / pharmacology*
HIV-1 / drug effects*
HIV-1 / genetics
HIV-1 / metabolism
Humans
Isoquinolines / pharmacology*
Molecular Sequence Data
Mutation
Quinolines / pharmacology*
Saquinavir
Valine / genetics
Viral Proteins / chemistry
Viral Proteins / genetics*

Substances

DNA Primers
HIV Protease Inhibitors
Isoquinolines
Quinolines
Viral Proteins
Valine
Saquinavir
Glycine