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An interactome map of the nucleocapsid protein from a highly pathogenic N orth A merican porcine reproductive and respiratory syndrome virus strain generated using SILAC ‐based quantitative proteomics
Author(s) -
Jourdan Stefanie S.,
Osorio Fernando,
Hiscox Julian A.
Publication year - 2012
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201100469
Subject(s) - biology , interactome , stable isotope labeling by amino acids in cell culture , porcine reproductive and respiratory syndrome virus , rna , virus , rna virus , virology , vp40 , viral structural protein , proteome , proteomics , microbiology and biotechnology , viral replication , gene , viral entry , genetics
Positive strand RNA viruses replicate in the cytoplasm of an infected cell and encode nucleocapsid proteins. These proteins function to promote encapsidation of the RNA genome and virus particle assembly as well as playing potential roles in viral RNA synthesis. Nucleocapsid proteins can also associate with cellular proteins and signaling cascades. The arterivirus nucleocapsid ( N ) protein is no exception and localizes to both the cytoplasm and the nucleolus in virus‐infected cells. This study generated an interactome map of the N protein from a highly virulent N orth A merican strain of porcine reproductive and respiratory syndrome virus ( PRRSV ). This is a major pathogen of swine resulting in significant morbidity and mortality. Crucial to the study was the use of SILAC coupled to affinity purification using GFP ‐traps and LC‐ MS /MS. This approach has not been applied before to the investigation of host/viral protein interactomes and this study revealed that the PRRSV N protein interacts with the host cell protein synthesis machinery especially at the level of translation initiation as well as with the RNA post‐transcriptional modification machinery. Applications of the dataset can include studies of virus/host interactions and the design of live attenuated recombinant vaccines.