Da. Croix et al., A DOMINANT EPITOPE OF HIV-1 PROTEASE RECOGNIZED BY HAMSTER MONOCLONAL-ANTIBODIES, Journal of acquired immune deficiency syndromes, 6(6), 1993, pp. 558-566
Monoclonal antibodies (mAbs) against HIV-1 protease (HIV PR), the esse
ntial protease of human immunodeficiency virus type 1 (HIV-1), were pr
oduced in Armenian hamsters. Studies of direct binding to synthetic pe
ptides and inhibition of binding to intact protease by peptide competi
tion showed that five mAbs recognized an epitope that includes the seq
uence LPGRWKPK (residues 38-45), which lies near the region of the pro
tease called the flap. All of the mAbs react specifically with HIV PR
in Western blots. Because of structural conservation of the epitope in
the proteases of many HIV-1 isolates, mAbs to this epitope are likely
to be useful for detection of HIV PR in field isolates of HIV-1. Also
, mAbs specific for this epitope, which lies close to the flap of HIV
PR, may be useful for functional studies of HIV PR and possibly for th
e design of inhibitors of protease activity that bind outside the enzy
me's catalytic site.