Volume 1 Issue 10
Oct.  2010
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Zhenhong Guan, Di Liu, Shuofu Mi, Jie Zhang, Qinong Ye, Ming Wang, George F. Gao, Jinghua Yan. Interaction of Hsp40 with influenza virus M2 protein: implications for PKR signaling pathway[J]. Protein&Cell, 2010, 1(10): 944-955. doi: 10.1007/s13238-010-0115-x
Citation: Zhenhong Guan, Di Liu, Shuofu Mi, Jie Zhang, Qinong Ye, Ming Wang, George F. Gao, Jinghua Yan. Interaction of Hsp40 with influenza virus M2 protein: implications for PKR signaling pathway[J]. Protein&Cell, 2010, 1(10): 944-955. doi: 10.1007/s13238-010-0115-x

Interaction of Hsp40 with influenza virus M2 protein: implications for PKR signaling pathway

doi: 10.1007/s13238-010-0115-x
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This work was supported by National Natural Sciences Foundation of China (NSFC) (Grant Nos. 30670091 and 30599434), National Basic Research Program (Project 973) of China Ministry of Science and Technology (Grant No. 2011CB504703), National Key Technologies R&D Program (Grant No. 2006BAD06A01). GFG is a leading principal investigator of the NSFC Innovative Research Group (Grant No. 81021003).

  • Received Date: 2010-09-25
  • Rev Recd Date: 2010-10-09
  • Influenza virus contains three integral membrane proteins:haemagglutinin, neuraminidase, and matrix protein (M1 and M2). Among them, M2 protein functions as an ion channel, important for virus uncoating in endosomes of virus-infected cells and essential for virus replication. In an effort to explore potential new functions of M2 in the virus life cycle, we used yeast two-hybrid system to search for M2-associated cellular proteins. One of the positive clones was identified as human Hsp40/Hdj1, a DnaJ/Hsp40 family protein. Here, we report that both BM2 (M2 of influenza B virus) and A/M2 (M2 of influenza A virus) interacted with Hsp40 in vitro and in vivo. The region of M2-Hsp40 interaction has been mapped to the CTD1 domain of Hsp40. Hsp40 has been reported to be a regulator of PKR signaling pathway by interacting with p58IPK that is a cellular inhibitor of PKR. PKR is a crucial component of the host defense response against virus infection. We therefore attempted to understand the relationship among M2, Hsp40 and p58IPK by further experimentation. The results demonstrated that both A/M2 and BM2 are able to bind to p58IPK in vitro and in vivo and enhance PKR autophosphorylation probably via forming a stable complex with Hsp40 and P58IPK, and consequently induce cell death. These results suggest that influenza virus M2 protein is involved in p58IPK mediated PKR regulation during influenza virus infection, therefore affecting infected-cell life cycle and virus replication.
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