tetano
Editor, Senior Moderator
Sci Rep. 2016 Feb 25;6:21845. doi: 10.1038/srep21845.
[h=1]Truncation of C-terminal 20 amino acids in PA-X contributes to adaptation of swine influenza virus in pigs.[/h] Xu G[SUP]1[/SUP], Zhang X[SUP]1[/SUP], Sun Y[SUP]1[/SUP], Liu Q[SUP]2[/SUP], Sun H[SUP]1[/SUP], Xiong X[SUP]1[/SUP], Jiang M[SUP]1[/SUP], He Q[SUP]1[/SUP], Wang Y[SUP]1[/SUP], Pu J[SUP]1[/SUP], Guo X[SUP]1[/SUP], Yang H[SUP]1[/SUP], Liu J[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The PA-X protein is a fusion protein incorporating the N-terminal 191 amino acids of the PA protein with a short C-terminal sequence encoded by an overlapping ORF (X-ORF) in segment 3 that is accessed by + 1 ribosomal frameshifting, and this X-ORF exists in either full length or a truncated form (either 61-or 41-condons). Genetic evolution analysis indicates that all swine influenza viruses (SIVs) possessed full-length PA-X prior to 1985, but since then SIVs with truncated PA-X have gradually increased and become dominant, implying that truncation of this protein may contribute to the adaptation of influenza virus in pigs. To verify this hypothesis, we constructed PA-X extended viruses in the background of a "triple-reassortment" H1N2 SIV with truncated PA-X, and evaluated their biological characteristics in vitro and in vivo. Compared with full-length PA-X, SIV with truncated PA-X had increased viral replication in porcine cells and swine respiratory tissues, along with enhanced pathogenicity, replication and transmissibility in pigs. Furthermore, we found that truncation of PA-X improved the inhibition of IFN-I mRNA expression. Hereby, our results imply that truncation of PA-X may contribute to the adaptation of SIV in pigs.
PMID: 26912401 [PubMed - in process]
[h=1]Truncation of C-terminal 20 amino acids in PA-X contributes to adaptation of swine influenza virus in pigs.[/h] Xu G[SUP]1[/SUP], Zhang X[SUP]1[/SUP], Sun Y[SUP]1[/SUP], Liu Q[SUP]2[/SUP], Sun H[SUP]1[/SUP], Xiong X[SUP]1[/SUP], Jiang M[SUP]1[/SUP], He Q[SUP]1[/SUP], Wang Y[SUP]1[/SUP], Pu J[SUP]1[/SUP], Guo X[SUP]1[/SUP], Yang H[SUP]1[/SUP], Liu J[SUP]1[/SUP].
[h=3]Author information[/h]
[h=3]Abstract[/h] The PA-X protein is a fusion protein incorporating the N-terminal 191 amino acids of the PA protein with a short C-terminal sequence encoded by an overlapping ORF (X-ORF) in segment 3 that is accessed by + 1 ribosomal frameshifting, and this X-ORF exists in either full length or a truncated form (either 61-or 41-condons). Genetic evolution analysis indicates that all swine influenza viruses (SIVs) possessed full-length PA-X prior to 1985, but since then SIVs with truncated PA-X have gradually increased and become dominant, implying that truncation of this protein may contribute to the adaptation of influenza virus in pigs. To verify this hypothesis, we constructed PA-X extended viruses in the background of a "triple-reassortment" H1N2 SIV with truncated PA-X, and evaluated their biological characteristics in vitro and in vivo. Compared with full-length PA-X, SIV with truncated PA-X had increased viral replication in porcine cells and swine respiratory tissues, along with enhanced pathogenicity, replication and transmissibility in pigs. Furthermore, we found that truncation of PA-X improved the inhibition of IFN-I mRNA expression. Hereby, our results imply that truncation of PA-X may contribute to the adaptation of SIV in pigs.
PMID: 26912401 [PubMed - in process]