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

Glycosylation of the Hemagglutinin Protein of H5N1 Influenza Virus Increases Its Virulence in Mice by Exacerbating the Host Immune Response

19 Jan 2017

Abstract excerpt

ABSTRACT The highly pathogenic avian influenza (HPAI) H5N1 viruses continue to circulate in nature and threaten public health. Although several viral determinants and host factors that influence the virulence of HPAI H5N1 viruses in mammals have been identified, the detailed molecular mechanism remains poorly defined and requires further clarification. In our previous studies, we characterized two naturally...

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 Influenza Virus Research Studies
Share to Respiratory viral infections research

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 28100622
DOI: 10.1128/jvi.02215-16

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

Glycosylation of the Hemagglutinin Protein of H5N1 Influenza Virus Increases Its Virulence in Mice by Exacerbating the Host Immune ResponsePMID 28100622Read ↗

The N-linked glycosylation site at position 158 on the head of hemagglutinin and the virulence of H5N1 avian influenza virus in mice.Semantic proximity Read ↗

N-linked glycosylation at site 158 of the HA protein of H5N6 highly pathogenic avian influenza virus is important for viral biological properties and host immune responsesSemantic proximity Read ↗

Glycosylation on hemagglutinin affects the virulence and pathogenicity of pandemic H1N1/2009 influenza A virus in mice.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 ↗

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

Genetic Requirement for Hemagglutinin Glycosylation and Its Implications for Influenza A H1N1 Virus EvolutionSemantic proximity Read ↗

Hemagglutinin glycosylation modulates the pathogenicity and antigenicity of the H5N1 avian influenza virusSemantic proximity Read ↗

N-linked glycosylation enhances hemagglutinin stability in avian H5N6 influenza virus to promote adaptation in mammalsSemantic proximity Read ↗

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

A Single Amino Acid at the Hemagglutinin Cleavage Site Contributes to the Pathogenicity and Neurovirulence of H5N1 Influenza Virus in MiceSemantic proximity Read ↗

The Multibasic Cleavage Site of the Hemagglutinin of Highly Pathogenic A/Vietnam/1203/2004 (H5N1) Avian Influenza Virus Acts as a Virulence Factor in a Host-Specific Manner in MammalsSemantic proximity Read ↗

N-Linked Glycosylation Attenuates H3N2 Influenza VirusesSemantic proximity Read ↗

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