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A Miniaturized Glycan Microarray Assay for Assessing Avidity and Specificity of Influenza A Virus Hemagglutinins
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Receptor binding by H10 influenza viruses
Sebastien G Vachieri1, Xiaoli Xiong1, Patrick J Collins2
11] MRC National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK [2].
Nature
|May 30, 2014
Summary
The H10N8 avian influenza virus shows high affinity for human receptors, posing a public health threat. While it can infect humans, its preference for avian receptors may limit widespread transmission.
Area of Science:
- Virology
- Public Health
- Structural Biology
Background:
- Avian influenza viruses, such as H5N1 and H7N9, pose significant public health risks due to their potential to infect humans.
- The H10N8 virus has recently emerged, with documented human cases and fatalities, necessitating an understanding of its epidemic potential.
Purpose of the Study:
- To investigate the epidemic potential of the H10N8 avian influenza virus.
- To determine the receptor-binding properties of the H10N8 virus haemagglutinin.
- To analyze the structural characteristics of H10N8 haemagglutinin in complex with human receptors.
Main Methods:
- Determination of the haemagglutinin structure of an avian H10 virus.
- Analysis of the receptor-binding properties of the H10 virus.
- Crystallographic studies of the avian H10 haemagglutinin complexed with human receptors.
Main Results:
- The H10N8 virus exhibits high avidity for human receptors.
- Structural analysis reveals that the bound human receptor conformation shares characteristics with both the 1918 H1N1 pandemic virus and human H7 viruses.
- The H10N8 virus has sufficient avidity for human receptors to cause human infections.
Conclusions:
- Avian H10N8 virus possesses the necessary avidity for human receptors to infect humans.
- The virus's preference for avian receptors may be counteracted by human airway mucins, potentially limiting widespread human-to-human transmission.
- Surveillance should focus on mutations in the H10 haemagglutinin's receptor-binding site that reduce avian receptor avidity, potentially increasing human transmissibility.
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