Journal
VETERINARY RESEARCH
Volume 48, Issue -, Pages -Publisher
BIOMED CENTRAL LTD
DOI: 10.1186/s13567-017-0410-0
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Funding
- China Postdoctoral Science Foundation [156471]
- Natural Science Foundation of Jiangsu Province [BK20130442]
- Postdoctoral Science Foundation of Jiangsu Province [1501075C]
- Open Project Program of Jiangsu Key Laboratory of Zoonosis [R1506]
- Yangzhou University Science and Technology Innovation Program [2015CXJ059]
- Earmarked Fund for Modern Agro-IndustryTechnology Research System [nycytx-41-G07]
- Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD)
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We generated and characterized site-directed HA mutants on the genetic backbone of H5N1 clade 2.3.4 virus preferentially binding to a-2,3 receptors in order to identify the key determinants in hemagglutinin rendering the dual affinity to both a-2,3 (avian-type) and a-2,6 (human-type) linked sialic acid receptors of the current clade 2.3.4.4 H5NX subtype avian influenza reassortants. The results show that the T160A substitution resulted in the loss of a glycosylation site at 158N and led not only to enhanced binding specificity for human-type receptors but also transmissibility among guinea pigs, which could be considered as an important molecular marker for assessing pandemic potential of H5 subtype avian influenza isolates.
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