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

Design and Expression of a Dimeric Form of Human Immunodeficiency Virus Type 1 Antibody 2G12 with Increased Neutralization Potency

23 Oct 2008

Abstract excerpt

The antigen-binding fragment of the broadly neutralizing human immunodeficiency virus type 1 (HIV-1) antibody 2G12 has an unusual three-dimensional (3D) domain-swapped structure with two aligned combining sites that facilitates recognition of its carbohydrate epitope on gp120. When expressed as an intact immunoglobulin G (IgG), 2G12 formed typical IgG monomers containing two combining sites and a small fraction...

Read the complete abstract on PubMed

Topics

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

Share to HIV Research and Treatment
Share to Immune Cell Function and Interaction
Share to Monoclonal and Polyclonal Antibodies Research

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Source

Identifiers

PMID: 18945777
DOI: 10.1128/jvi.01564-08

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 24 Oct 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Design and Expression of a Dimeric Form of Human Immunodeficiency Virus Type 1 Antibody 2G12 with Increased Neutralization PotencyPMID 18945777Read ↗

Antibody Domain Exchange Is an Immunological Solution to Carbohydrate Cluster RecognitionSemantic proximity Read ↗

Antibody 2G12 recognizes di-mannose equivalently in domain- and nondomain-exchanged forms but only binds the HIV-1 glycan shield if domain exchanged.Semantic proximity Read ↗

Human monoclonal antibody 2G12 defines a distinctive neutralization epitope on the gp120 glycoprotein of human immunodeficiency virus type 1.Semantic proximity Read ↗

Dimeric 2G12 as a Potent Protection against HIV-1Semantic proximity Read ↗

The Mannose-Dependent Epitope for Neutralizing Antibody 2G12 on Human Immunodeficiency Virus Type 1 Glycoprotein gp120Semantic proximity Read ↗

A dimeric form of the HIV-1 antibody 2G12 elicits potent antibody-dependent cellular cytotoxicity.Semantic proximity Read ↗

Bispecific Antibodies Targeting Different Epitopes on the HIV-1 Envelope Exhibit Broad and Potent NeutralizationSemantic proximity Read ↗

Immunofocusing: antigen engineering to promote the induction of HIV-neutralizing antibodies.Semantic proximity Read ↗

N-linked glycan modifications in gp120 of human immunodeficiency virus type 1 subtype C render partial sensitivity to 2G12 antibody neutralization.Semantic proximity Read ↗

Introduction of germline residues improves the stability of anti-HIV mAb 2G12-IgM.Semantic proximity Read ↗

Very Few Substitutions in a Germ Line Antibody Are Required To Initiate Significant Domain ExchangeSemantic proximity Read ↗

A Novel Human Antibody against Human Immunodeficiency Virus Type 1 gp120 Is V1, V2, and V3 Loop Dependent and Helps Delimit the Epitope of the Broadly Neutralizing Antibody Immunoglobulin G1 b12Semantic proximity Read ↗

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