Identification of an amino acid substitution involved in the reduction of sensitivity of HIV-1 to an inhibitor of viral proteinase.
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.
Turriziani
O
O
Institute of Virology, University La Sapienza, Rome, Italy.
Antonelli
G
G
Jacobsen
H
H
Mous
J
J
Riva
E
E
Pistello
M
M
Dianzani
F
F
D001483:Base Sequence; D017931:DNA Primers; D004352:Drug Resistance, Microbial / Q000235:genetics; D005998:Glycine / Q000235:genetics; D006678:HIV / Q000235:genetics / Q000378:metabolism; D017320:HIV Protease Inhibitors / Q000494:pharmacology*; D015497:HIV-1 / Q000187:drug effects* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D007546:Isoquinolines / Q000494:pharmacology*; D008969:Molecular Sequence Data; D009154:Mutation; D011804:Quinolines / Q000494:pharmacology*; D019258:Saquinavir; D014633:Valine / Q000235:genetics; D014764:Viral Proteins / Q000737:chemistry / Q000235:genetics*
D017931:DNA Primers; D017320:HIV Protease Inhibitors; D007546:Isoquinolines; D011804:Quinolines; D014764:Viral Proteins; D014633:Valine; D019258:Saquinavir; D005998:Glycine