Abstract:
:The unfolded protein response (UPR) in the endoplasmic reticulum (ER) constitutes a critical component of host innate immunity against microbial infections. In this report, we show that porcine reproductive and respiratory syndrome virus (PRRSV) utilizes the UPR machinery for its own benefit. We provide evidence that the virus targets the UPR central regulator GRP78 for proteasomal degradation via a mechanism that requires viral glycoprotein GP2a, while both IRE1-XBP1s and PERK-eIF2α-ATF4 signaling branches of the UPR are turned on at early stage of infection. The activated effector XBP1s was found to enter the nucleus, but ATF4 was unexpectedly diverted to cytoplasmic viral replication complexes by means of nonstructural proteins nsp2/3 to promote viral RNA synthesis. RNAi knockdown of either ATF4 or XBP1s dramatically attenuated virus titers, while overexpression caused increases. These observations reveal attractive host targets (e.g., ATF4 and XBP1s) for antiviral drugs and have implications in vaccine development.
journal_name
PLoS Pathogjournal_title
PLoS pathogensauthors
Gao P,Chai Y,Song J,Liu T,Chen P,Zhou L,Ge X,Guo X,Han J,Yang Hdoi
10.1371/journal.ppat.1008169subject
Has Abstractpub_date
2019-11-18 00:00:00pages
e1008169issue
11eissn
1553-7366issn
1553-7374pii
PPATHOGENS-D-19-00844journal_volume
15pub_type
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