Title |
Impact of amino acid substitutions in the V2 and C2 regions of human immunodeficiency virus type 1 CRF01_AE envelope glycoprotein gp120 on viral neutralization susceptibility to broadly neutralizing antibodies specific for the CD4 binding site
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Published in |
Retrovirology, April 2014
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DOI | 10.1186/1742-4690-11-32 |
Pubmed ID | |
Authors |
Piraporn Utachee, Panasda Isarangkura-na-ayuthaya, Kenzo Tokunaga, Kazuyoshi Ikuta, Naokazu Takeda, Masanori Kameoka |
Abstract |
The CD4 binding site (CD4bs) of envelope glycoprotein (Env) gp120 is a functionally conserved, important target of anti-human immunodeficiency virus type 1 (HIV-1) neutralizing antibodies. Two neutralizing human monoclonal antibodies, IgG1 b12 (b12) and VRC01, are broadly reactive neutralizing antibodies which recognize conformational epitopes that overlap the CD4bs of Env gp120; however, many CRF01_AE viruses are resistant to neutralization mediated by these antibodies. We examined the mechanism underlying the b12 resistance of the viruses using CRF01_AE Env (AE-Env)-recombinant viruses in this study. |
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