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

Binding of the hemagglutinin from human or equine influenza H3 viruses to the receptor is altered by substitutions at residue 193.

Archives of virology - 1 Aug 2004

Medeiros R, Naffakh N, Manuguerra J-C, van der Werf S

Abstract excerpt

Interactions of the hemagglutinin (HA) of influenza viruses with sialic acids (SA) are important for host range restriction. Most human H3s have a Ser193, while avian and equine H3s usually have an Asn or a Lys, respectively. To investigate the role of residue 193 in the recognition of SA, substitutions were introduced by mutagenesis within a human H3 and an equine H3. Hemadsorption assays performed on COS-1...

Read the complete abstract on PubMed

Topics

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

Share to Erythrocytes
Share to Guinea Pigs
Share to Hemagglutinin Glycoproteins, Influenza Virus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Horses

Share to Influenza A virus

Share to N-Acetylneuraminic Acid

Share to Receptors, Virus

Source

Identifiers

PMID: 15290389
DOI: 10.1007/s00705-003-0287-2

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Binding of the hemagglutinin from human or equine influenza H3 viruses to the receptor is altered by substitutions at residue 193.PMID 15290389Read ↗

Evolution of the receptor binding properties of the influenza A(H3N2) hemagglutininSemantic proximity Read ↗

Receptor binding specificity of recent human H3N2 influenza virusesSemantic proximity Read ↗

Structure and Receptor Binding Specificity of Hemagglutinin H13 from Avian Influenza A Virus H13N6Semantic proximity Read ↗

Recent avian H5N1 viruses exhibit increased propensity for acquiring human receptor specificity.Semantic proximity Read ↗

Early Alterations of the Receptor-Binding Properties of H1, H2, and H3 Avian Influenza Virus Hemagglutinins after Their Introduction into MammalsSemantic proximity Read ↗

Structures of receptor complexes formed by hemagglutinins from the Asian Influenza pandemic of 1957.Semantic proximity Read ↗

Haemagglutinin mutations responsible for the binding of H5N1 influenza A viruses to human-type receptors.Semantic proximity Read ↗

Identification of amino acid residues of influenza A virus H3 HA contributing to the recognition of molecular species of sialic acid.Semantic proximity Read ↗

H7 influenza A viruses bind sialyl-LewisX, a potential intermediate receptor between speciesSemantic proximity Read ↗

Quantitative description of glycan-receptor binding of influenza A virus H7 hemagglutinin.Semantic proximity Read ↗

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

An airborne transmissible avian influenza H5 hemagglutinin seen at the atomic level.Semantic proximity Read ↗

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