Active-site mutations in the South african human immunodeficiency virus type 1 subtype C protease have a significant impact on clinical inhibitor binding: kinetic and thermodynamic study.

Abstract:

:Human immunodeficiency virus (HIV) infections in sub-Saharan Africa represent about 56% of global infections. Study of active-site mutations (the V82A single mutation and the V82F I84V double mutation) in the less-studied South African HIV type 1 subtype C (C-SA) protease indicated that neither mutation had a significant impact on the proteolytic functioning of the protease. However, the binding affinities of, and inhibition by, saquinavir, ritonavir, indinavir, and nelfinavir were weaker for each variant than for the wild-type protease, with the double mutant exhibiting the most dramatic change. Therefore, our results show that the C-SA V82F I84V double mutation decreased the binding affinities of protease inhibitors to levels significantly lower than that required for effective inhibition.

journal_name

J Virol

journal_title

Journal of virology

authors

Mosebi S,Morris L,Dirr HW,Sayed Y

doi

10.1128/JVI.00726-08

subject

Has Abstract

pub_date

2008-11-01 00:00:00

pages

11476-9

issue

22

eissn

0022-538X

issn

1098-5514

pii

JVI.00726-08

journal_volume

82

pub_type

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