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

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

Archives of virology - 1 Feb 2015

Suptawiwat Ornpreya, Boonarkart Chompunuch, Chakritbudsabong Warunya, Uiprasertkul Mongkol, Puthavathana Pilaipan, Wiriyarat Witthawat, Auewarakul Prasert

Abstract excerpt

N-linked glycosylation of the influenza virus hemagglutinin (HA) protein plays crucial roles in HA structure and function, evasion of neutralizing antibodies, and susceptibility to innate soluble antiviral factors. The N-linked glycosylation site at position 158 of highly pathogenic H5N1 virus was previously shown to affect viral receptor-binding preference. H5N1 viruses show heterogeneity with respect to the...

Read the complete abstract on PubMed

Topics

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

Share to Glycosylation
Share to Hemagglutinin Glycoproteins, Influenza Virus

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Immune Evasion

Share to Influenza A Virus, H5N1 Subtype

Share to Madin Darby Canine Kidney Cells

Share to Orthomyxoviridae Infections

Share to Pulmonary Surfactant-Associated Protein D

Share to Virulence Factors

Source

Identifiers

PMID: 25504159
DOI: 10.1007/s00705-014-2306-x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The N-linked glycosylation site at position 158 on the head of hemagglutinin and the virulence of H5N1 avian influenza virus in mice.PMID 25504159Read ↗

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

N-Linked Glycosylation Attenuates H3N2 Influenza VirusesSemantic 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 ↗

Specific sites of N-linked glycosylation on the hemagglutinin of H1N1 subtype influenza A virus determine sensitivity to inhibitors of the innate immune system and virulence in mice.Semantic 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 ↗

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

Neuraminidase stalk length and additional glycosylation of the hemagglutinin influence the virulence of influenza H5N1 viruses for mice.Semantic proximity Read ↗

H9N2 Influenza Virus Infections in Human Cells Require a Balance between Neuraminidase Sialidase Activity and Hemagglutinin Receptor Affinity.Semantic proximity Read ↗

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

Mutations flanking the carbohydrate binding site of surfactant protein D confer antiviral activity for pandemic influenza A virusesSemantic proximity Read ↗

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

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