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

Epitope characterization of the protective monoclonal antibody VN04-2 shows broadly neutralizing activity against highly pathogenic H5N1.

Virology journal - 11 Jul 2008

Lim Angeline P C, Wong Steven K K, Chan Annie H Y, Chan Conrad E Z, Ooi Eng Eong, Hanson Brendon J

Abstract excerpt

The monoclonal antibody VN04-2 was previously shown to protect mice against lethal A/Vietnam/1203/04 H5N1 virus challenge when administered pre- and post-infection. In this study, we characterized the binding requirements of this antibody using direct binding to hemagglutinin and neutralization assays with H5N1 virus-like particles (H5N1-VLP) of eight recent H5N1 strains representing the major mutations within...

Read the complete abstract on PubMed

Topics

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

Share to Antibodies, Viral
Share to Antibody Specificity

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Epitopes

Share to Hemagglutinin Glycoproteins, Influenza Virus

Share to Indonesia

Share to Influenza A Virus, H5N1 Subtype

Share to Neutralization Tests

Share to Virion

Source

Open in PubMed Open full text

Identifiers

PMID: 18616831
DOI: 10.1186/1743-422X-5-80
PMCID: PMC2481255

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Epitope characterization of the protective monoclonal antibody VN04-2 shows broadly neutralizing activity against highly pathogenic H5N1.PMID 18616831Read ↗

Identification of a cross-neutralizing antibody that targets the receptor binding site of H1N1 and H5N1 influenza virusesSemantic proximity Read ↗

A highly conserved neutralizing epitope on group 2 influenza A viruses.Semantic proximity Read ↗

Reverse engineering the antigenic architecture of the haemagglutinin from influenza H5N1 clade 1 and 2.2 viruses with fine epitope mapping using monoclonal antibodies.Semantic proximity Read ↗

A Panel of Human Monoclonal Antibodies for Tracking the Antigenic Evolution of Influenza H5N1 Clade 2.3.4.4bSemantic proximity Read ↗

Human monoclonal antibodies that target clade 2.3.4.4b H5N1 hemagglutininSemantic proximity Read ↗

Potent efficacy of an NA-targeting antibody against a broad spectrum of H5N1 influenza viruses.Semantic proximity Read ↗

Human anti-N1 monoclonal antibodies elicited by pandemic H1N1 virus infection broadly inhibit HxN1 viruses in vitro and in vivoSemantic proximity Read ↗

Human protective monoclonal antibodies against the HA stem of group 2 HAs derived from an H3N2 virus-infected human.Semantic proximity Read ↗

A multimechanistic antibody targeting the receptor binding site potently cross-protects against influenza B virusesSemantic proximity Read ↗

A clade 2.3.4.4b H5N1 virus vaccine that elicits cross-protective antibodies against conserved domains of H5 and N1 glycoproteinsSemantic proximity Read ↗

Potent efficacy of a NA-targeting antibody against a broad spectrum of H5N1 influenza virusesSemantic proximity Read ↗

Generation of neutralizing and non-neutralizing monoclonal antibodies against H7N9 influenza virus.Semantic proximity Read ↗

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