Author: Sun, Di; Chen, Shun; Cheng, Anchun; Wang, Mingshu
Title: Roles of the Picornaviral 3C Proteinase in the Viral Life Cycle and Host Cells Document date: 2016_3_17
ID: 07nfb69o_10
Snippet: The cleavage specificity of 3C pro has largely been investigated via extensive sequence analysis of cleavage junctions in polyprotein and cleavage assays using protein or peptide substrates in vitro. Investigations have shown that the 3C pro of PV preferentially cleaves polypeptides with P1-Gln/P1'-Gly junctions. With the exception of FMDV 3C pro , other picornaviruses have less strict cleavage, with a small residue at P1', such as Gly, Ser, and .....
Document: The cleavage specificity of 3C pro has largely been investigated via extensive sequence analysis of cleavage junctions in polyprotein and cleavage assays using protein or peptide substrates in vitro. Investigations have shown that the 3C pro of PV preferentially cleaves polypeptides with P1-Gln/P1'-Gly junctions. With the exception of FMDV 3C pro , other picornaviruses have less strict cleavage, with a small residue at P1', such as Gly, Ser, and Ala or a hydrophobic residue at P4. The 3C pro of FMDV exhibits some variability at P1', however, the probability of P1-Gln or P1-Glu is similar [20] . Specific studies on the 3C pro of FMDV have shown that when P1-Gln is present, 3C pro prefers large hydrophobic residues at P1 (Leu, Ile, and Thr) and P2-Lys. Nonetheless, it is possible for a small amino acid (Gly and Ser) to be strongly associated with P1-Glu. The 3C pro of HAV can tolerate a large residue at P1 1 and exhibits a preference for a small hydrophilic residue at P2 [21] .
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