The Surface Glycoproteins of H5 Influenza Viruses Isolated from Humans, Chickens, and Wild Aquatic Birds Have Distinguishable Properties

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Journal of Virology, February 1999, p. 1146-1155, Vol. 73, No. 2
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

The Surface Glycoproteins of H5 Influenza Viruses Isolated from Humans, Chickens, and Wild Aquatic Birds Have Distinguishable Properties

Mikhail Matrosovich,¹^,²^,^* Nannan Zhou,¹^,³ Yoshihiro Kawaoka,⁴ and Robert Webster¹^,⁵

Department of Virology and Molecular Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105¹; M. P. Chumakov Institute of Poliomyelitis and Viral Encephalitides, 142 782 Moscow, Russia²; Department of Microbiology, Jiangxi Medical College, Nanchang 330006, China³; Department of Pathobiological Sciences, School of Veterinary Medicine, University of Wisconsin $---$ Madison, Madison, Wisconsin 53706⁴; and Department of Pathology, University of Tennessee at Memphis, Memphis, Tennessee 38163⁵

Received 7 August 1998/Accepted 20 October 1998

In 1997, 18 confirmed cases of human influenza arising from multiple independent transmissions of H5N1 viruses from infectedchickens were reported from Hong Kong. To identify possible phenotypicchanges in the hemagglutinin (HA) and neuraminidase (NA) of theH5 viruses during interspecies transfer, we compared the receptor-bindingproperties and NA activities of the human and chicken H5N1 isolatesfrom Hong Kong and of H5N3 and H5N1 viruses from wild aquaticbirds. All H5N1 viruses, including the human isolate bound toSia2-3Gal-containing receptors but not to Sia2-6Gal-containingreceptors. This finding formally demonstrates for the first timethat receptor specificity of avian influenza viruses may not restrictinitial avian-to-human transmission. The H5N1 chicken virusesdiffered from H5 viruses of wild aquatic birds by a 19-amino-aciddeletion in the stalk of the NA and the presence of a carbohydrateat the globular head of the HA. We found that a deletion in theNA decreased its ability to release the virus from cells, whereascarbohydrate at the HA head decreased the affinity of the virusfor cell receptors. Comparison of amino acid sequences from GenBankof the HAs and NAs from different avian species revealed thatadditional glycosylation of the HA and a shortened NA stalk arecharacteristic features of the H5 and H7 chicken viruses. Thisfinding indicates that changes in both HA and NA may be requiredfor the adaptation of influenza viruses from wild aquatic birdsto domestic chickens and raises the possibility that chickensmay be a possible intermediate host in zoonotictransmission.

^* Corresponding author. Mailing address: Department of Virology and Molecular Biology, St. Jude Children's Research Hospital,332 N. Lauderdale, Memphis, TN 38105. Phone: (901) 495-3412. Fax:(901) 523-2622. E-mail: Mikhail.Matrosovich{at}stjude.org.

Journal of Virology, February 1999, p. 1146-1155, Vol. 73, No. 2
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

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