tetano
Editor, Senior Moderator
Arch Virol. 2014 Dec 11. [Epub ahead of print]
[h=1]The N-linked glycosylation site at position 158 on the head of hemagglutinin and the virulence of H5N1 avian influenza virus in mice.[/h] Suptawiwat O[SUP]1[/SUP], Boonarkart C, Chakritbudsabong W, Uiprasertkul M, Puthavathana P, Wiriyarat W, Auewarakul P.
[h=3]Author information[/h]
[h=3]Abstract[/h] 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).
PMID: 25504159 [PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25504159
[h=1]The N-linked glycosylation site at position 158 on the head of hemagglutinin and the virulence of H5N1 avian influenza virus in mice.[/h] Suptawiwat O[SUP]1[/SUP], Boonarkart C, Chakritbudsabong W, Uiprasertkul M, Puthavathana P, Wiriyarat W, Auewarakul P.
[h=3]Author information[/h]
[h=3]Abstract[/h] 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).
PMID: 25504159 [PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25504159