A systematic study of the N-glycosylation sites of HIV-1 envelope protein on infectivity and antibody-mediated neutraliz
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A systematic study of the N-glycosylation sites of HIV-1 envelope protein on infectivity and antibody-mediated neutralization Retrovirology 2013, 10:14
doi:10.1186/1742-4690-10-14
Wenbo Wang ([email protected]) Jianhui Nie ([email protected]) Courtney Prochnow ([email protected]) Carolyn Truong ([email protected]) Zheng Jia ([email protected]) Suting Wang ([email protected]) Xiaojiang S Chen ([email protected]) Youchun Wang ([email protected])
ISSN Article type
1742-4690 Research
Submission date
5 September 2012
Acceptance date
4 February 2013
Publication date
6 February 2013
Article URL
http://www.retrovirology.com/content/10/1/14
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© 2013 Wang et al. This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
A systematic study of the N-glycosylation sites of HIV-1 envelope protein on infectivity and antibodymediated neutralization Wenbo Wang1 Email: [email protected] Jianhui Nie1 Email: [email protected] Courtney Prochnow2 Email: [email protected] Carolyn Truong2 Email: [email protected] Zheng Jia1 Email: [email protected] Suting Wang1 Email: [email protected] Xiaojiang S Chen2,3,4 Email: [email protected] Youchun Wang1* * Corresponding author Email: [email protected] 1
Department of Cell Biology, National Institutes for Food and Drug Control, No. 2 Tiantanxili, Beijing 100050, P. R. China 2
Department of Molecular and Computational Biology, University of Southern California, Los Angeles, CA 90089, USA 3
Chemistry Department, University of Southern California, Los Angeles, CA 90089, USA 4
Norris Cancer Center, University of Southern California, Los Angeles, CA 90089, USA
1
Abstract Background Glycans on the human immunodeficiency virus (HIV) envelope glycoprotein (Env) play an important role in viral infection and evasion of neutralization by antibodies. In this study, all 25 potential N-linked glycosylation sites (PNGS) on the HIV-1 CRF07_BC Env, FE, were mutated individually to study the effect of their removal on viral infectivity, virion production, and antibody-mediated neutralization.
Results Removal of specific N-glycosylation sites has a significant effect on viral infectivity and antibody-mediated neutralization phenotype. Six of these glycosylation mutants located on the V1/V2 and C1/C2 domains lost infectivity. PNGS mutations located on V4/C4/V5 (except N392 on V4), were shown to increase viral in
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