The 150-Loop Restricts the Host Specificity of Human H10N8 Influenza Virus

Netanel Tzarum, Robert P. de Vries, Wenjie Peng, Andrew J. Thompson, Kim M. Bouwman, Ryan McBride, Wenli Yu, Xueyong Zhu, Monique H. Verheije, James C. Paulson*, Ian A. Wilson

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

32 Scopus citations

Abstract

Adaptation of influenza A viruses to new hosts are rare events but are the basis for emergence of new influenza pandemics in the human population. Thus, understanding the processes involved in such events is critical for anticipating potential pandemic threats. In 2013, the first case of human infection by an avian H10N8 virus was reported, yet the H10 hemagglutinin (HA) maintains avian receptor specificity. However, the 150-loop of H10 HA, as well as related H7 and H15 subtypes, contains a two-residue insert that can potentially block human receptor binding. Mutation of the 150-loop on the background of Q226L and G228S mutations, which arose in the receptor-binding site of human pandemic H2 and H3 viruses, resulted in acquisition of human-type receptor specificity. Crystal structures of H10 HA mutants with human and avian receptor analogs, receptor-binding studies, and tissue staining experiments illustrate the important role of the 150-loop in H10 receptor specificity.

Original languageAmerican English
Pages (from-to)235-245
Number of pages11
JournalCell Reports
Volume19
Issue number2
DOIs
StatePublished - 11 Apr 2017
Externally publishedYes

Bibliographical note

Publisher Copyright:
© 2017 The Authors

Keywords

  • 150-loop
  • H10N8
  • HA
  • crystal structure
  • glycan array
  • hemagglutinin
  • host specificity
  • influenza A virus

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