A systematic study of the N-glycosylation sites of HIV-1 envelope protein on infectivity and antibody-mediated neutralization

@article{Wang2012ASS,
  title={A systematic study of the N-glycosylation sites of HIV-1 envelope protein on infectivity and antibody-mediated neutralization},
  author={Wen-bo Wang and J. Nie and Courtney Prochnow and C. Truong and Zheng Jia and Su-ting Wang and Xiaojiang S. Chen and Youchun Wang},
  journal={Retrovirology},
  year={2012},
  volume={10},
  pages={14 - 14}
}
BackgroundGlycans 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.ResultsRemoval of specific N-glycosylation sites has a significant effect on viral… Expand
N463 Glycosylation Site on V5 Loop of a Mutant gp120 Regulates the Sensitivity of HIV-1 to Neutralizing Monoclonal Antibodies VRC01/03
TLDR
The data indicate that N463 plays an important role in regulating the CD4bs MAbs VRC 01/VRC03 sensitivity in the genetic background of N197D mutation of gp120, which should provide valuable information for a better understanding of the interplay between HIV-1 and VRC01/03. Expand
The role of N-glycans of HIV-1 gp41 in virus infectivity and susceptibility to the suppressive effects of carbohydrate-binding agents
TLDR
The importance of some gp41 N-linked glycans, in particular the N616 glycan, was revealed to be absolutely indispensable for the infectivity potential of several virus strains and the antiviral activity of CBAs is not dependent on the concomitant presence of all gp41 glycans. Expand
The N276 Glycosylation Site Is Required for HIV-1 Neutralization by the CD4 Binding Site Specific HJ16 Monoclonal Antibody
TLDR
Data indicate that binding of the CD4bs specific HJ 16 mAb critically depends on the interaction with the N276-glycan, thus indicating that HJ16 is the first glycan dependentCD4bs-specific mAb. Expand
HIV-1 subtype C Envelope function becomes less sensitive to N-glycosylation deletion during disease progression
TLDR
Deletion of all PNGs significantly reduced TF entry efficiency, binding to dendritic cell-specific intracellular adhesion molecule 3 grabbing non-integrin receptor and trans-infection, and mutational analysis did not affect the phenotype of the CI Envelope to the same extent. Expand
Changes in Structure and Antigenicity of HIV-1 Env Trimers Resulting from Removal of a Conserved CD4 Binding Site-Proximal Glycan
TLDR
It is demonstrated that surgical glycosylation site modification may be an effective way of sculpting epitope presentation in Env-based vaccines by facilitating neutralizing antibody access to the CD4 binding site and modestly impacts the structural dynamics at the trimer crown without drastically altering global Env trimer stability. Expand
Glycosylation of the core of the HIV-1 envelope subunit protein gp120 is not required for native trimer formation or viral infectivity
TLDR
It is demonstrated that core gp120 glycans are not essential for folding, and hence their likely primary role is enabling immune evasion, and it is shown that the glycan removal approach is not strain restricted. Expand
Glycosylation in HIV-1 envelope glycoprotein and its biological implications
TLDR
This review provides an in-depth perspective of various aspects of Env glycosylation in the context of HIV-1 pathogenesis and may assist in effectively designing Env-based immunogens and in clearly understanding HIV vaccines. Expand
Functional and Structural Characterization of Human V3-Specific Monoclonal Antibody 2424 with Neutralizing Activity against HIV-1 JRFL
TLDR
A V3-specific monoclonal antibody that can completely neutralize HIV-1 JRFL, a virus isolate resistant to most V3 antibodies, is examined and it is revealed that this antibody recognizes the most distal tip of V3, which is not as occluded as other parts of V 3. Expand
The Impact of Mutations in SARS-CoV-2 Spike on Viral Infectivity and Antigenicity
  • Qianqian Li, Jiajing Wu, +17 authors Youchun Wang
  • Biology, Medicine
  • Cell
  • 2020
TLDR
Most variants with amino acid change at receptor binding domain were less infectious but variants including A475V, L452R, V483A and F490L became resistant to some neutralizing antibodies, while deletion of both N331 and N343 glycosylation drastically reduced infectivity, revealing the importance of gly cosylation for viral infectivity. Expand
Impact of glycan positioning on HIV-1 Env glycan shield density, function, and antibody recognition
TLDR
This study demonstrates how changes in individual glycan units can alter molecular dynamics and processing of the Env-glycan shield and, consequently, Env function. Expand
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