Abstract:
:Porcine epidemic diarrhea virus (PEDV), a member of the genus Alphacoronavirus, has caused significant damage to the Asian and American pork industries. Coronavirus 3C-like protease (3CL(pro)), which is involved in the processing of viral polyproteins for viral replication, is an appealing antiviral drug target. Here, we present the crystal structures of PEDV 3CL(pro) and a molecular complex between an inactive PEDV 3CL(pro) variant C144A bound to a peptide substrate. Structural characterization, mutagenesis and biochemical analysis reveal the substrate-binding pockets and the residues that comprise the active site of PEDV 3CL(pro). The dimerization of PEDV 3CL(pro) is similar to that of other Alphacoronavirus 3CL(pro)s but has several differences from that of SARS-CoV 3CL(pro) from the genus Betacoronavirus. Furthermore, the non-conserved motifs in the pockets cause different cleavage of substrate between PEDV and SARS-CoV 3CL(pro)s, which may provide new insights into the recognition of substrates by 3CL(pro)s in various coronavirus genera.
journal_name
Virologyjournal_title
Virologyauthors
Ye G,Deng F,Shen Z,Luo R,Zhao L,Xiao S,Fu ZF,Peng Gdoi
10.1016/j.virol.2016.04.018subject
Has Abstractpub_date
2016-07-01 00:00:00pages
225-35eissn
0042-6822issn
1096-0341pii
S0042-6822(16)30076-9journal_volume
494pub_type
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