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

Role of Sialic Acid Binding Specificity of the 1918 Influenza Virus Hemagglutinin Protein in Virulence and Pathogenesis for Mice

12 Feb 2009

Abstract excerpt

The 1918 influenza pandemic caused more than 40 million deaths and likely resulted from the introduction and adaptation of a novel avian-like virus. Influenza A virus hemagglutinins are important in host switching and virulence. Avian-adapted influenza virus hemagglutinins bind sialic acid receptors linked via alpha2-3 glycosidic bonds, while human-adapted hemagglutinins bind alpha2-6 receptors. Sequence analysis...

Read the complete abstract on PubMed

Topics

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

Share to Animal Disease Management and Epidemiology
Share to Immune Response and Inflammation
Share to Influenza Virus Research Studies

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 19211766
DOI: 10.1128/jvi.02596-08

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

Role of Sialic Acid Binding Specificity of the 1918 Influenza Virus Hemagglutinin Protein in Virulence and Pathogenesis for MicePMID 19211766Read ↗

Immunization by avian H5 influenza hemagglutinin mutants with altered receptor binding specificity.Semantic proximity Read ↗

N-Linked Glycosylation of the Hemagglutinin Protein Influences Virulence and Antigenicity of the 1918 Pandemic and Seasonal H1N1 Influenza A VirusesSemantic proximity Read ↗

A two-amino acid change in the hemagglutinin of the 1918 influenza virus abolishes transmission.Semantic proximity Read ↗

D225G mutation in hemagglutinin of pandemic influenza H1N1 (2009) virus enhances virulence in mice.Semantic proximity Read ↗

Altered receptor specificity and fusion activity of the haemagglutinin contribute to high virulence of a mouse-adapted influenza A virusSemantic proximity Read ↗

In vitro evolution of H5N1 avian influenza virus toward human-type receptor specificity.Semantic proximity Read ↗

N‐glycan structures of human alveoli provide insight into influenza A virus infection and pathogenesisSemantic proximity Read ↗

Mutation of the second sialic acid-binding site of influenza A virus neuraminidase drives compensatory mutations in hemagglutinin.Semantic proximity Read ↗

Sialic acid receptors: focus on their role in influenza infectionSemantic proximity Read ↗

An avian influenza H5N1 virus that binds to a human-type receptor.Semantic proximity Read ↗

Mutations during the adaptation of H7N9 avian influenza virus to mice lungs enhance human-like sialic acid binding activity and virulence in mice.Semantic proximity Read ↗

Highly Pathogenic Influenza A(H5Nx) Viruses with Altered H5 Receptor-Binding Specificity.Semantic proximity Read ↗

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