Amino Acid Substitutions That Affect Receptor Binding and Stability of the Hemagglutinin of Influenza A/H7N9 Virus

Eefje J A Schrauwen; Mathilde Richard; David F Burke; Guus F Rimmelzwaan; Sander Herfst; Ron A M Fouchier

doi:10.1128/JVI.03052-15

Amino Acid Substitutions That Affect Receptor Binding and Stability of the Hemagglutinin of Influenza A/H7N9 Virus

J Virol. 2016 Jan 20;90(7):3794-9. doi: 10.1128/JVI.03052-15.

Authors

Eefje J A Schrauwen¹, Mathilde Richard², David F Burke³, Guus F Rimmelzwaan¹, Sander Herfst¹, Ron A M Fouchier¹

Affiliations

¹ Department of Viroscience, Postgraduate School Molecular Medicine, Erasmus MC, Rotterdam, The Netherlands.
² Department of Viroscience, Postgraduate School Molecular Medicine, Erasmus MC, Rotterdam, The Netherlands m.richard@erasmusmc.nl.
³ Department of Zoology, University of Cambridge, Cambridge, United Kingdom.

Abstract

Receptor-binding preference and stability of hemagglutinin have been implicated as crucial determinants of airborne transmission of influenza viruses. Here, amino acid substitutions previously identified to affect these traits were tested in the context of an A/H7N9 virus. Some combinations of substitutions, most notably G219S and K58I, resulted in relatively high affinity for α2,6-linked sialic acid receptor and acid and temperature stability. Thus, the hemagglutinin of the A/H7N9 virus may adopt traits associated with airborne transmission.

Publication types

Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Substitution*
Cell Line
Hemagglutinin Glycoproteins, Influenza Virus / genetics
Hemagglutinin Glycoproteins, Influenza Virus / metabolism*
Humans
Influenza A Virus, H7N9 Subtype / genetics
Influenza A Virus, H7N9 Subtype / physiology*
Mutant Proteins / genetics
Mutant Proteins / metabolism
Sialic Acids / metabolism
Temperature
Virus Attachment*

Substances

Hemagglutinin Glycoproteins, Influenza Virus
Mutant Proteins
Sialic Acids

Associated data

PDB/4LN6

Grants and funding

EU FP7 provided funding to Eefje J. A. Schrauwen, Mathilde Richard, Guus F Rimmelzwaan, Sander Herfst, and Ron A. M. Fouchier under grant number 278976 (7th Framework Programme ANTIGONE).