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Journal of Virology, January 2004, p. 502-507, Vol. 78, No. 1
0022-538X/04/$08.00+0 DOI: 10.1128/JVI.78.1.502-507.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
Restrictions to the Adaptation of Influenza A Virus H5 Hemagglutinin to the Human Host
Ruth Harvey,1,2,
Andrew C. R. Martin,1 Maria Zambon,2 and Wendy S. Barclay1*
School of Animal and Microbial Sciences, University of Reading, Reading RG6 6AJ,1
Health Protection Agency, Enteric and Respiratory Virus Laboratory, Colindale, London NW9 5HT, United Kingdom2
Received 30 June 2003/
Accepted 17 September 2003
The binding specificities of a panel of avian influenza virus subtype H5 hemagglutinin (HA) proteins bearing mutations at key residues in the receptor binding site were investigated. The results demonstrate that two simultaneous mutations in the receptor binding site resulted in H5 HA binding in a pattern similar to that shown by human viruses. Coexpression of the ion channel protein, M2, from most avian and human strains tested protected H5 HA conformation during trafficking, indicating that no genetic barrier to the reassortment of the H5 surface antigen gene with internal genes of human viruses existed at this level.
* Corresponding author. Mailing address: School of Animal and Microbial Sciences, P.O. Box 228, Whiteknights, University of Reading, Reading RG6 6AJ, United Kingdom. Phone: 44 1189 316368. Fax: 44 1189 316671. E-mail:
w.s.barclay{at}reading.ac.uk.
Present address: Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom.
Journal of Virology, January 2004, p. 502-507, Vol. 78, No. 1
0022-538X/04/$08.00+0 DOI: 10.1128/JVI.78.1.502-507.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
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