Publication: The N-linked glycosylation site at position 158 on the head of hemagglutinin and the virulence of H5N1 avian influenza virus in mice
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Issued Date
2014-01-01
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03048608
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2-s2.0-84925486400
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Mahidol University
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SCOPUS
Bibliographic Citation
Archives of Virology. Vol.160, No.2 (2014), 409-415
Suggested Citation
Ornpreya Suptawiwat, Chompunuch Boonarkart, Warunya Chakritbudsabong, Mongkol Uiprasertkul, Pilaipan Puthavathana, Witthawat Wiriyarat, Prasert Auewarakul The N-linked glycosylation site at position 158 on the head of hemagglutinin and the virulence of H5N1 avian influenza virus in mice. Archives of Virology. Vol.160, No.2 (2014), 409-415. doi:10.1007/s00705-014-2306-x Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/34006
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Title
The N-linked glycosylation site at position 158 on the head of hemagglutinin and the virulence of H5N1 avian influenza virus in mice
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Abstract
© 2014, Springer-Verlag Wien. N-linked glycosylation of the influenza virus hemagglutinin (HA) protein plays crucial roles in HA structure and function, evasion of neutralizing antibodies, and susceptibility to innate soluble antiviral factors. The N-linked glycosylation site at position 158 of highly pathogenic H5N1 virus was previously shown to affect viral receptor-binding preference. H5N1 viruses show heterogeneity with respect to the presence of this glycosylation site. Clade 1 viruses that caused outbreaks in Southeast Asia in 2004 contained this glycosylation site, while the site is absent in the more recent clade 2 viruses. Here, we show that elimination of this glycosylation site increases viral virulence in mice. The mutant lacking the glycosylation site at position 158 showed unaltered growth kinetics in vitro and a comparable level of sensitivity to a major antiviral protein found in respiratory secretions, surfactant protein D (SP-D).