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Article

Hemagglutinin glycosylation modulates the pathogenicity and antigenicity of the H5N1 avian influenza virus

20 Dec 2014

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Identifiers

PMID: 25544041
DOI: 10.1016/j.vetmic.2014.12.011

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Hemagglutinin glycosylation modulates the pathogenicity and antigenicity of the H5N1 avian influenza virusPMID 25544041Read ↗

Glycosylation and an amino acid insertion in the head of hemagglutinin independently affect the antigenic properties of H5N1 avian influenza virusesSemantic proximity Read ↗

The evolution of hemagglutinin-158 and neuraminidase-88 glycosylation sites modulates antigenicity and pathogenicity of clade 2.3.2.1 H5N1 avian influenza virusesSemantic proximity Read ↗

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

Addition of N-glycosylation sites on the globular head of the H5 hemagglutinin induces the escape of highly pathogenic avian influenza A H5N1 viruses from vaccine-induced immunitySemantic proximity Read ↗

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

N-glycosylation on hemagglutinin head reveals inter-branch antigenic variability of avian influenza virus H5-subtypesSemantic proximity Read ↗

Effects of Glycosylation on the Properties and Functions of Influenza Virus HemagglutininSemantic proximity Read ↗

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

Structural features of the avian influenza virus hemagglutinin that influence virulenceSemantic proximity Read ↗

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