Title | Comparative influenza protein interactomes identify the role of plakophilin 2 in virus restriction |
Authors | Wang, Lingyan Fu, Bishi Li, Wenjun Patil, Girish Liu, Lin Dorf, Martin E. Li, Shitao |
Affiliation | Oklahoma State Univ, Dept Physiol Sci, 264 McELroy Hall, Stillwater, OK 74078 USA. Harvard Med Sch, Dept Microbiol & Immunobiol, 77 Ave Louis Pasteur,NRB830, Boston, MA 02115 USA. Peking Univ, Sch Stomatol, 22 Zhongguancun South Ave, Beijing 100081, Peoples R China. |
Keywords | PATTERN-RECOGNITION RECEPTORS 2009 PANDEMIC H1N1 NF-KAPPA-B A VIRUS RNA-POLYMERASE NS1 PROTEIN INTERACTION NETWORK PROTEOMIC ANALYSIS ARMADILLO FAMILY STRUCTURAL BASIS |
Issue Date | 2017 |
Publisher | NATURE COMMUNICATIONS |
Citation | NATURE COMMUNICATIONS.2017,8. |
Abstract | Cellular protein interaction networks are integral to host defence and immune signalling pathways, which are often hijacked by viruses via protein interactions. However, the comparative virus-host protein interaction networks and how these networks control host immunity and viral infection remain to be elucidated. Here, we mapped protein interactomes between human host and several influenza A viruses (IAV). Comparative analyses of the interactomes identified common and unique interaction patterns regulating innate immunity and viral infection. Functional screening of the 'core' interactome consisting of common interactions identified five novel host factors regulating viral infection. Plakophilin 2 (PKP2), an influenza PB1-interacting protein, restricts IAV replication and competes with PB2 for PB1 binding. The binding competition leads to perturbation of the IAV polymerase complex, thereby limiting polymerase activity and subsequent viral replication. Taken together, comparative analyses of the influenza-host protein interactomes identified PKP2 as a natural inhibitor of IAV polymerase complex. |
URI | http://hdl.handle.net/20.500.11897/475204 |
ISSN | 2041-1723 |
DOI | 10.1038/ncomms13876 |
Indexed | SCI(E) |
Appears in Collections: | 口腔医院 |