tetano
Editor, Senior Moderator
J Biotechnol
. 2020 Aug 18;S0168-1656(20)30222-4.
doi: 10.1016/j.jbiotec.2020.08.009. Online ahead of print.
A novel SUMOylation site in the influenza a virus NS1 protein identified with a highly sensitive FRET assay
George Way[SUP] 1 [/SUP], Zhehao Xiong[SUP] 1 [/SUP], Guojun Wang[SUP] 2 [/SUP], Hanchu Dai[SUP] 3 [/SUP], Shasha Zheng[SUP] 3 [/SUP], Adolfo Garc?a-Sastre[SUP] 4 [/SUP], Jiayu Liao[SUP] 5 [/SUP]
Affiliations
Abstract
Nonstructural protein 1 (NS1) of the influenza A virus is a major contributor to the virulence of the seasonal influenza A viruses, in part because it interferes with host viral defense mechanisms. SUMOylation regulates NS1 activity, and several residues of NS1 have been identified with traditional biochemical approaches as acceptor sites for SUMOylation. In this study, we developed a novel FRET assay to assess SUMOylation. Using this assay, we demonstrated that the lysine residue K131 in the effector domain of NS1 is a previously unidentified SUMO acceptor site. A recombinant H1N1 influenza A virus (A/PR/8/34) expressing a K131 SUMOylation-deficient NS1 had a significantly lower growth rate than the wild-type virus. These results suggest that NS1 SUMOylation at K131 is required for the rapid replication of H1N1 influenza viruses. The interaction between the NS1 protein and the host SUMOylation components may serve as a novel target for the development of anti-influenza A drugs.
Keywords: FRET; H1N1; NS1 influenza A virus; SUMOylation.
. 2020 Aug 18;S0168-1656(20)30222-4.
doi: 10.1016/j.jbiotec.2020.08.009. Online ahead of print.
A novel SUMOylation site in the influenza a virus NS1 protein identified with a highly sensitive FRET assay
George Way[SUP] 1 [/SUP], Zhehao Xiong[SUP] 1 [/SUP], Guojun Wang[SUP] 2 [/SUP], Hanchu Dai[SUP] 3 [/SUP], Shasha Zheng[SUP] 3 [/SUP], Adolfo Garc?a-Sastre[SUP] 4 [/SUP], Jiayu Liao[SUP] 5 [/SUP]
Affiliations
- PMID: 32822681
- DOI: 10.1016/j.jbiotec.2020.08.009
Abstract
Nonstructural protein 1 (NS1) of the influenza A virus is a major contributor to the virulence of the seasonal influenza A viruses, in part because it interferes with host viral defense mechanisms. SUMOylation regulates NS1 activity, and several residues of NS1 have been identified with traditional biochemical approaches as acceptor sites for SUMOylation. In this study, we developed a novel FRET assay to assess SUMOylation. Using this assay, we demonstrated that the lysine residue K131 in the effector domain of NS1 is a previously unidentified SUMO acceptor site. A recombinant H1N1 influenza A virus (A/PR/8/34) expressing a K131 SUMOylation-deficient NS1 had a significantly lower growth rate than the wild-type virus. These results suggest that NS1 SUMOylation at K131 is required for the rapid replication of H1N1 influenza viruses. The interaction between the NS1 protein and the host SUMOylation components may serve as a novel target for the development of anti-influenza A drugs.
Keywords: FRET; H1N1; NS1 influenza A virus; SUMOylation.