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Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
agricultural and biological sciences
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
Journal of Virology, Volume 82, No. 22, Year 2008
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Description
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. Copyright © 2008, American Society for Microbiology. All Rights Reserved.
Authors & Co-Authors
Mosebi, Salerwe
South Africa, Johannesburg
University of the Witwatersrand
Morris, Lynn
South Africa, Johannesburg
National Institute for Communicable Diseases
Dirr, Heini W.
South Africa, Johannesburg
University of the Witwatersrand
Sayed, Yasien
South Africa, Johannesburg
University of the Witwatersrand
Statistics
Citations: 42
Authors: 4
Affiliations: 2
Identifiers
Doi:
10.1128/JVI.00726-08
ISSN:
0022538X
Research Areas
Cancer
Infectious Diseases