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

Files in This Work
There are no files associated with this item.

Web of Science®


0

Checked on Last Week

Scopus®



Checked on Current Time

百度学术™


0

Checked on Current Time

Google Scholar™





License: See PKU IR operational policies.