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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/34006
Title: The N-linked glycosylation site at position 158 on the head of hemagglutinin and the virulence of H5N1 avian influenza virus in mice
Authors: Ornpreya Suptawiwat
Chompunuch Boonarkart
Warunya Chakritbudsabong
Mongkol Uiprasertkul
Pilaipan Puthavathana
Witthawat Wiriyarat
Prasert Auewarakul
Mahidol University
Keywords: Immunology and Microbiology
Issue Date: 1-Jan-2014
Citation: Archives of Virology. Vol.160, No.2 (2014), 409-415
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).
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84925486400&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/34006
ISSN: 03048608
Appears in Collections:Scopus 2011-2015

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