Twenty amino acids at the C-terminus of PA-X are associated with increased influenza A virus replication and pathogenicityTools Gao, Huijie, Sun, Yipeng, Liu, Xiufan, Sun, Honglei, Hu, Jiao, Wang, Jinliang, Lin, Yang, Chang, Kin-Chow, Wang, Yu, Qi, Lu, Pu, Juan, Xiong, Xin, Liu, Jinhua, Seng, Lai-Giea, Kong, Weili and He, Qiming (2015) Twenty amino acids at the C-terminus of PA-X are associated with increased influenza A virus replication and pathogenicity. Journal of General Virology, 96 (8). pp. 2036-2049. ISSN 0022-1317 Full text not available from this repository.
Official URL: https://doi.org/10.1099/vir.0.000143
AbstractThe PA-X protein, arising from ribosomal frameshift during PA translation, was recently discovered in influenza A virus (IAV). The C-terminal domain ‘X’ of PA-X proteins in IAVs can be classified as full-length (61 aa) or truncated (41 aa). In the main, avian influenza viruses express full-length PA-X proteins, whilst 2009 pandemic H1N1 (pH1N1) influenza viruses harbour truncated PA proteins. The truncated form lacks aa 232–252 of the full-length PA-X protein. The significance of PA-X length in virus function remains unclear. To address this issue, we constructed a set of contemporary influenza viruses (pH1N1, avian H5N1 and H9N2) with full and truncated PA-X by reverse genetics to compare their replication and host pathogenicity. All full-length PA-X viruses in human A549 cells conferred 10- to 100-fold increase in viral replication and 5–8 % increase in apoptosis relative to corresponding truncated PA-X viruses. Full-length PA-X viruses were more virulent and caused more severe inflammatory responses in mice. Furthermore, aa 233–252 at the C terminus of PA-X strongly suppressed co-transfected gene expression by ∼50 %, suggesting that these terminal 20 aa could play a role in enhancing viral replication and contribute to virulence.
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