| Literature DB >> 32351035 |
Sujuan Chen1,2,3,4, Yizhang Xie1,2,3,4, Xiang Su1,2,3,4, Jing Xue1,2,3,4, Xiao Wang1,2,3,4, Yinping Du1,2,3,4, Tao Qin1,2,3,4, Daxin Peng1,2,3,4, Xiufan Liu1,2,3,4.
Abstract
The influenza A virus (IAV) PB2 subunit modulates viral polymerase activity, replication kinetics and pathogenicity. Here we identified novel PB2 substitutions at position 283 of H5 subtype IAV and evaluated their biological characteristics and virulence. The substitution PB2-M283L enhanced the growth capacity and polymerase activity in human and mammalian cells in comparison to the rWT virus. The substitution PB2-M283L displayed high virulence, resulting in a greater virus load in different tissues, more severe histopathological lesions and proinflammatory cytokines burst in mice. The substitution PB2-M283I had an opposite phenotype. Our data extend the important role of PB2 substitutions in the adaptation of H5 subtype IAVs to mammalian hosts.Entities:
Keywords: PB2; PB2-M283L/I; influenza A viruses; virulence
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Year: 2020 PMID： 32351035 DOI： 10.1111/tbed.13601
Source DB: PubMed Journal: Transbound Emerg Dis ISSN： 1865-1674 Impact factor: 5.005