Receptor Specificity and Transmission of H2N2 Subtype Viruses Isolated from the Pandemic of 1957

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Receptor Specificity and Transmission of H2N2 Subtype Viruses Isolated from the Pandemic of 1957

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Title: Receptor Specificity and Transmission of H2N2 Subtype Viruses Isolated from the Pandemic of 1957
Author: Pappas, Claudia; Viswanathan, Karthik; Chandrasekaran, Aarthi; Raman, Rahul; Katz, Jacqueline M.; Tumpey, Terrence M.; Sasisekharan, Ram

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Citation: Pappas, Claudia, Karthik Viswanathan, Aarthi Chandrasekaran, Rahul Raman, Jacqueline M. Katz, Ram Sasisekharan, and Terrence M. Tumpey. 2010. Receptor specificity and transmission of H2N2 subtype viruses isolated from the pandemic of 1957. PLoS ONE 5(6): e11158.
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Abstract: Influenza viruses of the H2N2 subtype have not circulated among humans in over 40 years. The occasional isolation of avian H2 strains from swine and avian species coupled with waning population immunity to H2 hemagglutinin (HA) warrants investigation of this subtype due to its pandemic potential. In this study we examined the transmissibility of representative human H2N2 viruses, A/Albany/6/58 (Alb/58) and A/El Salvador/2/57 (ElSalv/57), isolated during the 1957/58 pandemic, in the ferret model. The receptor binding properties of these H2N2 viruses was analyzed using dose-dependent direct glycan array-binding assays. Alb/58 virus, which contains the 226L/228S amino acid combination in the HA and displayed dual binding to both alpha 2,6 and alpha 2,3 glycan receptors, transmitted efficiently to naïve ferrets by respiratory droplets. Inefficient transmission was observed with ElSalv/57 virus, which contains the 226Q/228G amino acid combination and preferentially binds alpha 2,3 over alpha 2,6 glycan receptors. However, a unique transmission event with the ElSalv/57 virus occurred which produced a 226L/228G H2N2 natural variant virus that displayed an increase in binding specificity to alpha 2,6 glycan receptors and enhanced respiratory droplet transmissibility. Our studies provide a correlation between binding affinity to glycan receptors with terminal alpha 2,6-linked sialic acid and the efficiency of respiratory droplet transmission for pandemic H2N2 influenza viruses.
Published Version: doi:10.1371/journal.pone.0011158
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2888575/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:4768787

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