Two N-linked glycosylation sites in the V2 and C2 regions of human immunodeficiency virus type 1 CRF01_AE envelope glycoprotein gp120 regulate viral neutralization susceptibility to the human monoclonal antibody specific for the CD4 binding domain.

@article{Utachee2010TwoNG,
  title={Two N-linked glycosylation sites in the V2 and C2 regions of human immunodeficiency virus type 1 CRF01_AE envelope glycoprotein gp120 regulate viral neutralization susceptibility to the human monoclonal antibody specific for the CD4 binding domain.},
  author={Piraporn Utachee and Shota Nakamura and Panasda Isarangkura-na-ayuthaya and Kenzo Tokunaga and Pathom Sawanpanyalert and Kazuyoshi Ikuta and Wattana Auwanit and Masanori Kameoka},
  journal={Journal of virology},
  year={2010},
  volume={84 9},
  pages={4311-20}
}
A recombinant human monoclonal antibody, IgG1 b12 (b12), recognizes a conformational epitope on human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein (Env) gp120 that overlaps the CD4 binding domain. Although b12 is able to broadly neutralize HIV-1 subtype B, C, and D viruses, many HIV-1 CRF01_AE viruses are resistant to b12-mediated neutralization. In this report, we examined the molecular mechanisms underlying the low neutralization susceptibility of CRF01_AE viruses to b12, using… CONTINUE READING

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