The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade.
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Activity of and effect of subcutaneous treatment with the broad-spectrum antiviral lectin griffithsin in two laboratory rodent modelsThe HIV glycan shield as a target for broadly neutralizing antibodiesRecent strategies targeting HIV glycans in vaccine designA Blueprint for HIV Vaccine DiscoveryDesigning synthetic vaccines for HIVVaccine-Elicited Tier 2 HIV-1 Neutralizing Antibodies Bind to Quaternary Epitopes Involving Glycan-Deficient Patches Proximal to the CD4 Binding SiteComplex-type N-glycan recognition by potent broadly neutralizing HIV antibodiesBroadly Neutralizing Antibody PGT121 Allosterically Modulates CD4 Binding via Recognition of the HIV-1 gp120 V3 Base and Multiple Surrounding GlycansStructural basis for diverse N-glycan recognition by HIV-1–neutralizing V1–V2–directed antibody PG16Structural Basis for Enhanced HIV-1 Neutralization by a Dimeric Immunoglobulin G Form of the Glycan-Recognizing Antibody 2G12Targeting host-derived glycans on enveloped viruses for antibody-based vaccine designStructural Constraints Determine the Glycosylation of HIV-1 Envelope TrimersCell- and Protein-Directed Glycosylation of Native Cleaved HIV-1 EnvelopeGlycan clustering stabilizes the mannose patch of HIV-1 and preserves vulnerability to broadly neutralizing antibodiesGlycans, galectins, and HIV-1 infectionImmunogenicity of Stabilized HIV-1 Envelope Trimers with Reduced Exposure of Non-neutralizing EpitopesA next-generation cleaved, soluble HIV-1 Env trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodiesPharmacokinetics of the Antiviral Lectin Griffithsin Administered by Different Routes Indicates Multiple Potential UsesAllosteric modulation of the HIV-1 gp120-gp41 association site by adjacent gp120 variable region 1 (V1) N-glycans linked to neutralization sensitivityComposition and Antigenic Effects of Individual Glycan Sites of a Trimeric HIV-1 Envelope GlycoproteinHigh-throughput profiling of anti-glycan humoral responses to SIV vaccination and challengeStructural plasticity of the Semliki Forest virus glycome upon interspecies transmission.HIV-1 Glycan Density Drives the Persistence of the Mannose Patch within an Infected Individual.MALDI-MS/MS with traveling wave ion mobility for the structural analysis of N-linked glycans.Vaccine Elicitation of High Mannose-Dependent Neutralizing Antibodies against the V3-Glycan Broadly Neutralizing Epitope in Nonhuman PrimatesSynthetic carbohydrate antigens for HIV vaccine design.Antibody to gp41 MPER alters functional properties of HIV-1 Env without complete neutralizationHIV-1 envelope proteins and V1/V2 domain scaffolds with mannose-5 to improve the magnitude and quality of protective antibody responses to HIV-1Differential glycosylation of envelope gp120 is associated with differential recognition of HIV-1 by virus-specific antibodies and cell infection.Glycosylation and disulfide bond analysis of transiently and stably expressed clade C HIV-1 gp140 trimers in 293T cells identifies disulfide heterogeneity present in both proteins and differences in O-linked glycosylationPartial enzymatic deglycosylation preserves the structure of cleaved recombinant HIV-1 envelope glycoprotein trimers.Glycoform and net charge heterogeneity in gp120 immunogens used in HIV vaccine trials.Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: An update for 2011-2012.Prime-boost immunization of rabbits with HIV-1 gp120 elicits potent neutralization activity against a primary viral isolate.Broadly neutralizing antibodies suppress HIV in the persistent viral reservoirHIV-1 envelope glycan moieties modulate HIV-1 transmission.Structural evolution of glycan recognition by a family of potent HIV antibodies.Two classes of broadly neutralizing antibodies within a single lineage directed to the high-mannose patch of HIV envelopeDeletion of the highly conserved N-glycan at Asn260 of HIV-1 gp120 affects folding and lysosomal degradation of gp120, and results in loss of viral infectivityGp120 on HIV-1 Virions Lacks O-Linked Carbohydrate.
P2860
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P2860
The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade.
description
2011 nî lūn-bûn
@nan
2011 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
The glycan shield of HIV is pr ...... duction system or viral clade.
@ast
The glycan shield of HIV is pr ...... duction system or viral clade.
@en
type
label
The glycan shield of HIV is pr ...... duction system or viral clade.
@ast
The glycan shield of HIV is pr ...... duction system or viral clade.
@en
prefLabel
The glycan shield of HIV is pr ...... duction system or viral clade.
@ast
The glycan shield of HIV is pr ...... duction system or viral clade.
@en
P2093
P2860
P1433
P1476
The glycan shield of HIV is pr ...... oduction system or viral clade
@en
P2093
Camille Bonomelli
Christopher N Scanlan
D Cameron Dunlop
Dennis R Burton
Raymond A Dwek
Victoria Thaney
P2860
P304
P356
10.1371/JOURNAL.PONE.0023521
P407
P577
2011-08-16T00:00:00Z