Tuesday, June 11, 2013

Glycan Receptor Binding of the Influenza A Virus H7N9 Hemagglutinin

[This is the publication of the "Cell" which the article I posted at the blog below is referring to]
Cell, 06 June 2013



  • Highlights
  • The hemagglutinin of H7N9 virus does not efficiently bind human receptors
  • A single residue change in receptor binding site increases binding to human receptors
  • Mutations on hemagglutinin may reduce the effectiveness of current H7 vaccines


The advent of H7N9 in early 2013 is of concern for a number of reasons, including its capability to infect humans, the lack of clarity in the etiology of infection, and because the human population does not have pre-existing immunity to the H7 subtype. Earlier sequence analyses of H7N9 hemagglutinin (HA) point to amino acid changes that predicted human receptor binding and impinge on the antigenic characteristics of the HA. Here, we report that the H7N9 HA shows limited binding to human receptors; however, should a single amino acid mutation occur, this would result in structural changes within the receptor binding site that allow for extensive binding to human receptors present in the upper respiratory tract. Furthermore, a subset of the H7N9 HA sequences demarcating coevolving amino acids appears to be in the antigenic regions of H7, which, in turn, could impact effectiveness of the current WHO-recommended prepandemic H7 vaccines.


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