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The T160A hemagglutinin substitution affects not only receptor binding property but also transmissibility of H5N1 clade 2.3.4 avian influenza virus in guinea pigs.

ABSTRACT: We generated and characterized site-directed HA mutants on the genetic backbone of H5N1 clade 2.3.4 virus preferentially binding to ?-2,3 receptors in order to identify the key determinants in hemagglutinin rendering the dual affinity to both ?-2,3 (avian-type) and ?-2,6 (human-type) linked sialic acid receptors of the current clade 2.3.4.4 H5NX subtype avian influenza reassortants. The results show that the T160A substitution resulted in the loss of a glycosylation site at 158N and led not only to enhanced binding specificity for human-type receptors but also transmissibility among guinea pigs, which could be considered as an important molecular marker for assessing pandemic potential of H5 subtype avian influenza isolates.

SUBMITTER: Gu M 

PROVIDER: S-EPMC5294818 | biostudies-literature | 2017 Feb

REPOSITORIES: biostudies-literature

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The T160A hemagglutinin substitution affects not only receptor binding property but also transmissibility of H5N1 clade 2.3.4 avian influenza virus in guinea pigs.

Gu Min M   Li Qunhui Q   Gao Ruyi R   He Dongchang D   Xu Yunpeng Y   Xu Haixu H   Xu Lijun L   Wang Xiaoquan X   Hu Jiao J   Liu Xiaowen X   Hu Shunlin S   Peng Daxin D   Jiao Xinan X   Liu Xiufan X  

Veterinary research 20170206 1

We generated and characterized site-directed HA mutants on the genetic backbone of H5N1 clade 2.3.4 virus preferentially binding to α-2,3 receptors in order to identify the key determinants in hemagglutinin rendering the dual affinity to both α-2,3 (avian-type) and α-2,6 (human-type) linked sialic acid receptors of the current clade 2.3.4.4 H5NX subtype avian influenza reassortants. The results show that the T160A substitution resulted in the loss of a glycosylation site at 158N and led not only  ...[more]

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