Publication: An avian influenza H5N1 virus that binds to a human-type receptor
2
Issued Date
2007-09-01
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ISSN
0022538X
Other identifier(s)
2-s2.0-35348895001
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Mahidol University
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SCOPUS
Bibliographic Citation
Journal of Virology. Vol.81, No.18 (2007), 9950-9955
Suggested Citation
Prasert Auewarakul, Ornpreya Suptawiwat, Alita Kongchanagul, Chak Sangma, Yasuo Suzuki, Kumnuan Ungchusak, Suda Louisirirotchanakul, Hatairat Lerdsamran, Phisanu Pooruk, Arunee Thitithanyanont, Chakrarat Pittayawonganon, Chao Tan Guo, Hiroaki Hiramatsu, Wipawee Jampangern, Supamit Chunsutthiwat, Pilaipan Puthavathana An avian influenza H5N1 virus that binds to a human-type receptor. Journal of Virology. Vol.81, No.18 (2007), 9950-9955. doi:10.1128/JVI.00468-07 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/24515
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Title
An avian influenza H5N1 virus that binds to a human-type receptor
Author(s)
Prasert Auewarakul
Ornpreya Suptawiwat
Alita Kongchanagul
Chak Sangma
Yasuo Suzuki
Kumnuan Ungchusak
Suda Louisirirotchanakul
Hatairat Lerdsamran
Phisanu Pooruk
Arunee Thitithanyanont
Chakrarat Pittayawonganon
Chao Tan Guo
Hiroaki Hiramatsu
Wipawee Jampangern
Supamit Chunsutthiwat
Pilaipan Puthavathana
Ornpreya Suptawiwat
Alita Kongchanagul
Chak Sangma
Yasuo Suzuki
Kumnuan Ungchusak
Suda Louisirirotchanakul
Hatairat Lerdsamran
Phisanu Pooruk
Arunee Thitithanyanont
Chakrarat Pittayawonganon
Chao Tan Guo
Hiroaki Hiramatsu
Wipawee Jampangern
Supamit Chunsutthiwat
Pilaipan Puthavathana
Abstract
Avian influenza viruses preferentially recognize sialosugar chains terminating in sialic acid-α2,3-galactose (SAα2,3Gal), whereas human influenza viruses preferentially recognize SAα2,6Gal. A conversion to SAα2,6Gal 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 SAα2,3Gal to both SAα2,3Gal and SAα2,6Gal. Molecular modeling demonstrated that the mutation may stabilize SAα2,6Gal 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. Copyright © 2007, American Society for Microbiology. All Rights Reserved.