Journal
VIROLOGY
Volume 446, Issue 1-2, Pages 349-356Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2013.08.011
Keywords
Influenza virus; Tissue tropism; Virulence; Receptor specificity; Replication
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Funding
- Intramural Research Program of the National Institute of Allergy and Infectious Diseases (NIAID)
- National Institutes of Health (NIH)
- National Institutes of Health [R37 GM057073-13]
- Singapore-MIT Alliance for Research and Technology (SMART)
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Human influenza viruses predominantly bind alpha 2,6 linked sialic acid (SA) while avian viruses bind alpha 2,3 SA-containing complex glycans. Virulence and tissue tropism of influenza viruses have been ascribed to this binding preference. We generated 2009 pandemic H1N1 (pH1N1) viruses with either predominant alpha 2,3 or alpha 2,6 SA binding and evaluated these viruses in mice and ferrets. The alpha 2,3 pH1N1 virus had similar virulence in mice and replicated to similar titers in the respiratory tract of mice and ferrets as the alpha 2,6 and WT pH1N1 viruses. Immunohistochemical analysis determined that all viruses infected similar cell types in ferret lungs. There is increasing evidence that receptor specificity of influenza viruses is more complex than the binary model of alpha 2,6 and alpha 2,3 SA binding and our data suggest that influenza viruses use a wide range of SA moieties to infect host cells. Published by Elsevier Inc.
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