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

Fitness costs limit influenza A virus hemagglutinin glycosylation as an immune evasion strategy.

Proceedings of the National Academy of Sciences of the United States of America - 20 Dec 2011

Das Suman R, Hensley Scott E, David Alexandre, Schmidt Loren, Gibbs James S, Puigbò Pere, Ince William L, Bennink Jack R, Yewdell Jonathan W

Abstract excerpt

Here, we address the question of why the influenza A virus hemagglutinin (HA) does not escape immunity by hyperglycosylation. Uniquely among dozens of monoclonal antibodies specific for A/Puerto Rico/8/34, escape from H28-A2 neutralization requires substitutions introducing N-linked glycosylation at residue 131 or 144 in the globular domain. This escape decreases viral binding to cellular receptors, which must be...

Read the complete abstract on PubMed

Topics

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

Share to Antigens
Share to Dogs

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

Share to Epitope Mapping

Share to Glycosylation

Share to Hemagglutinins

Share to Immune System

Share to Influenza A virus

Share to Molecular Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 22106257
DOI: 10.1073/pnas.1108754108
PMCID: PMC3251056

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 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

Fitness costs limit influenza A virus hemagglutinin glycosylation as an immune evasion strategy.PMID 22106257Read ↗

Hemagglutinin receptor binding avidity drives influenza A virus antigenic drift.Semantic proximity Read ↗

N-linked glycans on influenza A H3N2 hemagglutinin constrain binding of host antibodies, but shielding is limited.Semantic proximity Read ↗

Influenza A virus hemagglutinin glycosylation compensates for antibody escape fitness costsSemantic proximity Read ↗

Glycosylations in the Globular Head of the Hemagglutinin Protein Modulate the Virulence and Antigenic Properties of the H1N1 Influenza VirusesSemantic proximity Read ↗

Glycan shielding of the influenza virus hemagglutinin contributes to immunopathology in mice.Semantic proximity Read ↗

Addition of N-glycosylation sites on the globular head of the H5 hemagglutinin induces the escape of highly pathogenic avian influenza A H5N1 viruses from vaccine-induced immunitySemantic proximity Read ↗

Human Influenza A Virus Hemagglutinin Glycan Evolution Follows a Temporal Pattern to a Glycan LimitSemantic proximity Read ↗

A Perspective on the Structural and Functional Constraints for Immune Evasion: Insights from Influenza Virus.Semantic proximity Read ↗

Glycan remodeled erythrocytes facilitate antigenic characterization of recent A/H3N2 influenza virusesSemantic proximity Read ↗

Glycan remodeled erythrocytes facilitate antigenic characterization of recent A/H3N2 influenza virusesSemantic proximity Read ↗

Addition of glycosylation to influenza A virus hemagglutinin modulates antibody-mediated recognition of H1N1 2009 pandemic viruses.Semantic proximity Read ↗

Loss of hemagglutination ability by H3N2 influenza A virus, subclade KSemantic proximity Read ↗

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