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. 2021 Oct 13;12:757451. doi: 10.3389/fmicb.2021.757451

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Copyright © 2021 Zhang, Li, Cao, Wang, Wang, Xie, Gao, Fu, Zhou and Wu.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Analyses of cleavage sites in the N-terminus of P2 regions of MaPV and ApGlV1 using in vitro trans-cleavage assays. (A) Schematic representation of the expressed substrates and the expressed proteases. MaPV-P2_1–310 and ApGlV1_1–199 were used as the substrates, and MBP-MaPV-Pro_1094–1490-SUMO-His and MBP-ApGlV1-Pro_956–1355-SUMO-His were used as the proteases. The calculated molecular mass of individual cleaved products is indicated. The predicted cleavage sites are shown as described in Figure 9. (B) In vitro trans-cleavage analysis of the N-terminus of P2 regions of MaPV and their mutants. The indicated amino acids in the mutants were mutated to AA. (C) In vitro trans-cleavage analysis of the N-terminus of P2 regions of ApGlV1 and their mutants. The indicated amino acids in the mutants were mutated to AA.