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Journal of Virology, September 2007, p. 9950-9955, Vol. 81, No. 18
0022-538X/07/$08.00+0     doi:10.1128/JVI.00468-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

An Avian Influenza H5N1 Virus That Binds to a Human-Type Receptor{triangledown}

Prasert Auewarakul,1* Ornpreya Suptawiwat,1 Alita Kongchanagul,1 Chak Sangma,6 Yasuo Suzuki,7 Kumnuan Ungchusak,4 Suda Louisirirotchanakul,1 Hatairat Lerdsamran,1 Phisanu Pooruk,1 Arunee Thitithanyanont,2 Chakrarat Pittayawonganon,4 Chao-Tan Guo,7 Hiroaki Hiramatsu,7 Wipawee Jampangern,3 Supamit Chunsutthiwat,5 and Pilaipan Puthavathana1

Faculty of Medicine, Siriraj Hospital,1 Faculty of Science,2 Faculty of Tropical Medicine,3 Mahidol University, Bangkok, Thailand; Bureau of Epidemiology,4 Department of Disease Control, Bangkok, Thailand,5 Faculty of Science, Kasetsart University, Bangkok, Thailand,6 College of Life and Health Sciences, Chubu University, Kasugai, Japan7

Received 5 March 2007/ Accepted 18 June 2007

Avian influenza viruses preferentially recognize sialosugar chains terminating in sialic acid-{alpha}2,3-galactose (SA{alpha}2,3Gal), whereas human influenza viruses preferentially recognize SA{alpha}2,6Gal. A conversion to SA{alpha}2,6Gal specificity is believed to be one of the changes required for the introduction of new hemagglutinin (HA) subtypes to the human population, which can lead to pandemics. Avian influenza H5N1 virus is a major threat for the emergence of a pandemic virus. As of 12 June 2007, the virus has been reported in 45 countries, and 312 human cases with 190 deaths have been confirmed. We describe here substitutions at position 129 and 134 identified in a virus isolated from a fatal human case that could change the receptor-binding preference of HA of H5N1 virus from SA{alpha}2,3Gal to both SA{alpha}2,3Gal and SA{alpha}2,6Gal. Molecular modeling demonstrated that the mutation may stabilize SA{alpha}2,6Gal in its optimal cis conformation in the binding pocket. The mutation was found in approximately half of the viral sequences directly amplified from a respiratory specimen of the patient. Our data confirm the presence of H5N1 virus with the ability to bind to a human-type receptor in this patient and suggest the selection and expansion of the mutant with human-type receptor specificity in the human host environment.

* Corresponding author. Mailing address: Department of Microbiology, Faculty of Medicine, Siriraj Hospital, Mahidol University, Bangkok 10700, Thailand. Phone: 662 4197068. Fax: 662 4184148. E-mail: sipaw{at}mahidol.ac.th

{triangledown} Published ahead of print on 11 July 2007.

Journal of Virology, September 2007, p. 9950-9955, Vol. 81, No. 18
0022-538X/07/$08.00+0     doi:10.1128/JVI.00468-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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