Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Viral resistance to VRC01-like antibodies with mutations in loop D and V5 from an HIV-1 B' subtype infected individual with broadly neutralization activity.

Molecular immunology - 1 May 2022

Zhang Dai, Liu Zhen, Wang Wei, Chen Ming-Xin, Hou Jia-Li, Zhang Zhen, Ren Wei-Hong, Ren Li, Hao Yan-Ling

Abstract excerpt

Recently we identified the VRC01-like antibody DRVIA7(A7) from an HIV-1 B' subtype-infected individual (DRVI01) with broad neutralization activity, and almost all viruses from the individual were resistant to both VRC01 and A7 lineage antibodies. Here, we identified and characterized a panel of HIV-1 variants with resistance to VRC01 and A7 using site-directed mutagenesis and swapping amino acid fragments of...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Antibodies, Monoclonal
Share to Antibodies, Neutralizing

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to HIV Antibodies

Share to HIV Envelope Protein gp120

Share to HIV Infections

Share to Mutation

Source

Identifiers

PMID: 35290812
DOI: 10.1016/j.molimm.2022.02.021

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Viral resistance to VRC01-like antibodies with mutations in loop D and V5 from an HIV-1 B' subtype infected individual with broadly neutralization activity.PMID 35290812Read ↗

A single residue within the V5 region of HIV-1 envelope facilitates viral escape from the broadly neutralizing monoclonal antibody VRC01.Semantic proximity Read ↗

Resistance mutations that distinguish HIV-1 envelopes with discordant VRC01 phenotypes from multi-lineage infections in the HVTN703/HPTN081 trial: implications for cross-resistance.Semantic proximity Read ↗

De novo identification of VRC01 class HIV-1-neutralizing antibodies by next-generation sequencing of B-cell transcripts.Semantic proximity Read ↗

Structural basis for germline gene usage of a potent class of antibodies targeting the CD4 binding site of HIV-1 gp120Semantic proximity Read ↗

Dual role of glycosylation in resistance to CD4-binding site broadly neutralizing antibodies.Semantic proximity Read ↗

Comprehensive Cross-Clade Neutralization Analysis of a Panel of Anti-Human Immunodeficiency Virus Type 1 Monoclonal AntibodiesSemantic proximity Read ↗

Rational Design of Envelope Identifies Broadly Neutralizing Human Monoclonal Antibodies to HIV-1Semantic proximity Read ↗

Structural basis for germ-line gene usage of a potent class of antibodies targeting the CD4-binding site of HIV-1 gp120Semantic proximity Read ↗

Structure of an N276-Dependent HIV-1 Neutralizing Antibody Targeting a Rare V5 Glycan Hole Adjacent to the CD4 Binding SiteSemantic proximity Read ↗

Identification of a novel broadly HIV-1-neutralizing antibody from a CRF01_AE-infected Chinese donorSemantic proximity Read ↗

Glycans flanking the hypervariable connecting peptide between the A and B strands of the V1/V2 domain of HIV-1 gp120 confer resistance to antibodies that neutralize CRF01_AE viruses.Semantic proximity Read ↗

N463 Glycosylation Site on V5 Loop of a Mutant gp120 Regulates the Sensitivity of HIV-1 to Neutralizing Monoclonal Antibodies VRC01/03.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.