Archary, Derseree.Rong, Rong.Gordon, Michelle Lucille.Boliar, Saikat.Madiga, Maphuti C.Gray, Elin Solomonovna.Dugast, Anne-Sophie.Hermanus, Tandile.Goulder, Philip Jeremy Renshaw.Coovadia, Hoosen Mahomed.Werner, Lise.Morris, Lynn.Alter, Galit.Derdeyn, Cynthia A.Ndung'u, Peter Thumbi.2013-07-022013-07-0220122012Archary, D. et al. 2012. Characterization of anti-HIV-1 neutralizing and binding antibodies in chronic HIV-1 subtype C infection. Virology 433 (2) pp. 410-420.0042-6822http://dx.doi.org/10.1016/j.virol.2012.08.033http://hdl.handle.net/10413/9243Neutralizing (nAbs) and high affinity binding antibodies may be critical for an efficacious HIV-1 vaccine. We characterized virus-specific nAbs and binding antibody responses over 21 months in eight HIV-1 subtype C chronically infected individuals with heterogeneous rates of disease progression. Autologous nAb titers of study exit plasma against study entry viruses were significantly higher than contemporaneous responses at study entry (p=0.002) and exit (p=0.01). NAb breadth and potencies against subtype C viruses were significantly higher than for subtype A (p=0.03 and p=0.01) or B viruses (p=0.03; p=0.05) respectively. Gp41-IgG binding affinity was higher than gp120-IgG (p=0.0002). IgG–FcγR1 affinity was significantly higher than FcγRIIIa (p<0.005) at study entry and FcγRIIb (p<0.05) or FcγRIIIa (p<0.005) at study exit. Evolving IgG binding suggests alteration of immune function mediated by binding antibodies. Evolution of nAbs was a potential marker of HIV-1 disease progression.enHIV infections--Virology.AIDS vaccines.Neutralizing antibodies.Binding antibodies.HIV-1 subtype C.Peer reviewed journal article