THARAKARAMAN K, Raman R, Viswanathan K, Stebbins N. Structural determinants for naturally evolving H5N1 hemagglutinin to switch its receptor specificity. Cell. 2013 Jun 20;153(7):1475-85.
Of the factors governing human-to-human transmission of the highly pathogenic avian-adapted H5N1 virus, the most critical is the acquisition of mutations on the viral hemagglutinin (HA) to "quantitatively switch" its binding from avian to human glycan receptors. Here, we describe a structural framework that outlines a necessary set of H5 HA receptor-binding site (RBS) features required for the H5 HA to quantitatively switch its preference to human receptors. We show here that the same RBS HA mutations that lead to aerosol transmission of A/Vietnam/1203/04 and A/Indonesia/5/05 viruses, when introduced in currently circulating H5N1, do not lead to a quantitative switch in receptor preference. We demonstrate that HAs from circulating clades require as few as a single base pair mutation to quantitatively switch their binding to human receptors. The mutations identified by this study can be used to monitor the emergence of strains having human-to-human transmission potential
See Also:
Latest articles in those days:
- [preprint] Emergence and interstate spread of highly pathogenic avian influenza A(H5N1) in dairy cattle 23 hours ago
- Modelling the transmission dynamics of H9N2 avian influenza viruses in a live bird market 23 hours ago
- CD8+ T-cell responses towards conserved influenza B virus epitopes across anatomical sites and age 3 days ago
- Surveillance for highly pathogenic avian influenza A (H5N1) in a raptor rehabilitation center-2022 4 days ago
- [preprint]Detection of hemagglutinin H5 influenza A virus sequence in municipal wastewater solids at wastewater treatment plants with increases in influenza A in spring, 2024 4 days ago
[Go Top] [Close Window]