Structural highlights
Function
[NS2A_CVMA5] Not essential for virus replication in transformed murine cells.
Publication Abstract from PubMed
Prior studies have demonstrated that the mouse hepatitis virus A59 strain (MHV-A59) ns2 protein is a member of the 2H phosphoesterase family and exhibits 2',5'-phosphodiesterase (2',5'-PDE) activity. During the interferon antiviral response, ns2 cleaves 2',5'-oligoadenylate (2-5A), a key mediator of RNase L activation, thereby subverting the activation of RNase L and evading host innate immunity. However, the mechanism of 2-5A cleavage by ns2 remains unclear. Here, we present the crystal structure of the MHV ns2 PDE domain and demonstrate a PDE fold similar to that of the cellular protein, a kinase anchoring protein 7 central domain (AKAP7CD) and rotavirus VP3 carboxy-terminal domain (VP3-CTD). The structure displays a pair of strictly conserved HxS/Tx motifs and forms a deep positively charged catalytic groove with beta-sheets and an arginine containing loop (R-loop). These findings provide insight into the structural basis for 2-5A binding of MHV ns2.
Crystal structure of the mouse hepatitis virus ns2 phosphodiesterase domain that antagonizes RNase L activation.,Sui B, Huang J, Jha BK, Yin P, Zhou M, Fu ZF, Silverman RH, Weiss SR, Peng G, Zhao L J Gen Virol. 2016 Jan 12. doi: 10.1099/jgv.0.000395. PMID:26757803[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sui B, Huang J, Jha BK, Yin P, Zhou M, Fu ZF, Silverman RH, Weiss SR, Peng G, Zhao L. Crystal structure of the mouse hepatitis virus ns2 phosphodiesterase domain that antagonizes RNase L activation. J Gen Virol. 2016 Jan 12. doi: 10.1099/jgv.0.000395. PMID:26757803 doi:https://dx.doi.org/10.1099/jgv.0.000395
