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

Very Few Substitutions in a Germ Line Antibody Are Required To Initiate Significant Domain Exchange

12 Aug 2010

Abstract excerpt

2G12 is a broadly neutralizing anti-HIV-1 monoclonal human IgG1 antibody reactive with a high-mannose glycan cluster on the surface of glycoprotein gp120. A key feature of this very highly mutated antibody is domain exchange of the heavy-chain variable region (V(H)) with the V(H) of the adjacent Fab of the same immunoglobulin, which assembles a multivalent binding interface composed of two primary binding sites...

Read the complete abstract on PubMed

Topics

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

Share to Galectins and Cancer Biology
Share to Glycosylation and Glycoproteins Research
Share to Monoclonal and Polyclonal Antibodies Research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 20702640
DOI: 10.1128/jvi.01111-10

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

Very Few Substitutions in a Germ Line Antibody Are Required To Initiate Significant Domain ExchangePMID 20702640Read ↗

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 ↗

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

An Insertion Mutation That Distorts Antibody Binding Site Architecture Enhances Function of a Human AntibodySemantic proximity Read ↗

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

Structural basis for HIV-1 gp120 recognition by a germ-line version of a broadly neutralizing antibody.Semantic proximity Read ↗

Differential reactivity of germ line allelic variants of a broadly neutralizing HIV-1 antibody to a gp41 fusion intermediate conformation.Semantic proximity Read ↗

Cooperation between somatic mutation and germline-encoded residues enables antibody recognition of HIV-1 envelope glycans.Semantic proximity Read ↗

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

Conserved amino acid networks involved in antibody variable domain interactionsSemantic 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 ↗

P04-05. Requirements for antibody domain exchange explored through mutation of the germline 2G12 antibodySemantic proximity Read ↗

Dependence on a variable residue limits the breadth of an HIV MPER neutralizing antibody, despite convergent evolution with broadly neutralizing antibodiesSemantic proximity Read ↗

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