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

A Single Mutation at Position 190 in Hemagglutinin Enhances Binding Affinity for Human Type Sialic Acid Receptor and Replication of H9N2 Avian Influenza Virus in Mice.

Journal of virology - 1 Nov 2016

Teng Qiaoyang, Xu Dawei, Shen Weixia, Liu Qinfang, Rong Guangyu, Li Xuesong, Yan Liping, Yang Jianmei, Chen Hongjun, Yu Hai, Ma Wenjun, Li Zejun

Abstract excerpt

H9N2 avian influenza virus (AIV) has an extended host range, but the molecular basis underlying H9N2 AIV transmission to mammals remains unclear. We isolated more than 900 H9N2 AIVs in our 3-year surveillance in live bird markets in China from 2009 to 2012. Thirty-seven representative isolates were selected for further detailed characterization. These isolates were categorized into 8 genotypes (B64 to B71) and...

Read the complete abstract on PubMed

Topics

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

Share to A549 Cells
Share to Birds

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Hemagglutinin Glycoproteins, Influenza Virus

Share to Influenza A Virus, H9N2 Subtype

Share to Influenza, Human

Share to Influenza in Birds

Share to Orthomyxoviridae Infections

Share to Virus Attachment

Source

Open in PubMed Open full text

Identifiers

PMID: 27558420
DOI: 10.1128/JVI.01141-16
PMCID: PMC5068531

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

A Single Mutation at Position 190 in Hemagglutinin Enhances Binding Affinity for Human Type Sialic Acid Receptor and Replication of H9N2 Avian Influenza Virus in Mice.PMID 27558420Read ↗

Enhanced pathogenicity and transmissibility of H9N2 avian influenza virus in mammals by hemagglutinin mutations combined with PB2-627K.Semantic proximity Read ↗

The S190R mutation in the hemagglutinin protein of pandemic H1N1 2009 influenza virus increased its pathogenicity in mice.Semantic proximity Read ↗

Evolution and Adaptation of the Avian H7N9 Virus into the Human HostSemantic proximity Read ↗

Influenza A (H6N6) virus isolated from chickens replicate in mice and human lungs without prior adaptationSemantic proximity Read ↗

A single-amino-acid mutation at position 225 in hemagglutinin attenuates H5N6 influenza virus in miceSemantic proximity Read ↗

The host tropism of current zoonotic H7N9 viruses depends mainly on an acid-labile hemagglutinin with a single amino acid mutation in the stalk region.Semantic proximity Read ↗

Avian-to-Human Receptor-Binding Adaptation of Avian H7N9 Influenza Virus HemagglutininSemantic proximity Read ↗

Dual receptor-binding, infectivity, and transmissibility of an emerging H2N2 low pathogenicity avian influenza virus.Semantic proximity Read ↗

Global distribution, receptor binding, and cross-species transmission of H6 influenza viruses: risks and implications for humansSemantic proximity Read ↗

Impact of Mutations in the Hemagglutinin of H10N7 Viruses Isolated from Seals on Virus Replication in Avian and Human Cells.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 ↗

Molecular characterization and receptor binding specificity of H9N2 avian influenza viruses based on poultry-related environmental surveillance in China between 2013 and 2016Semantic proximity Read ↗

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