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A Miniaturized Glycan Microarray Assay for Assessing Avidity and Specificity of Influenza A Virus Hemagglutinins
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A Miniaturized Glycan Microarray Assay for Assessing Avidity and Specificity of Influenza A Virus Hemagglutinins

Published on: May 29, 2016

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Glycosylation changes in the globular head of H3N2 influenza hemagglutinin modulate receptor binding without

Irina V Alymova1, Ian A York1, Gillian M Air2

  • 1Influenza Division, National Center for Immunization & Respiratory Diseases, Centers for Disease Control &Prevention, Atlanta, GA, USA.

Scientific Reports
|November 1, 2016
PubMed

Insights

Human H3N2 influenza A viruses show reduced severity linked to changes in hemagglutinin (HA) glycosylation and receptor binding. This study suggests these binding changes did not cause the reduced virulence, offering insights into influenza virulence factors.

Area of Science:

  • Virology
  • Immunology
  • Molecular Biology

Background:

  • Human H3N2 influenza A viruses, emerging in 1968, are now moderate severity strains.
  • Virulence decline correlates with increased hemagglutinin (HA) glycosylation and altered glycan receptor binding specificity.
  • The link between HA glycosylation, binding changes, and reduced H3N2 virulence remains unclear.

Purpose of the Study:

  • To investigate the impact of hemagglutinin glycosylation on receptor binding and virulence in engineered H3N2 influenza viruses.
  • To determine if altered glycan binding specificity contributes to the decreased severity of seasonal H3N2 viruses.

Main Methods:

  • Engineering H3N2 influenza viruses with varying HA glycosylation patterns.
  • Assessing receptor binding affinities of engineered viruses to different glycan structures.
  • Evaluating the virulence of engineered H3N2 viruses in relevant models.

Main Results:

  • Engineered low-binding H3N2 virus exhibited virulence comparable to higher-binding counterparts.
  • H3N2 infection does not necessitate broad glycan receptor recognition or high-avidity binding.
  • Two specific glycan structures were recognized by most H3N2 viruses from 1968-2012, suggesting conserved physiologically relevant binding.

Conclusions:

  • Altered hemagglutinin binding specificity did not contribute to the reduced severity of seasonal H3N2 influenza viruses.
  • Physiologically relevant H3N2 hemagglutinin binding has remained consistent since the 1968 pandemic.
  • This research guides the identification of factors influencing influenza virus virulence.

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