Front. Microbiol. Frontiers in Microbiology Front. Microbiol. 1664-302X Frontiers Media S.A. 10.3389/fmicb.2017.01762 Microbiology Correction Corrigendum: Identification of Cleavage Sites Recognized by the 3C-Like Cysteine Protease within the Two Polyproteins of Strawberry Mottle Virus Mann Krin S. Walker Melanie C. Sanfaçon Hélène * Agriculture and Agri-Food Canada, Summerland Research and Development Centre Summerland, BC, Canada

Edited and reviewed by: Nobuhiro Suzuki, Okayama University, Japan

*Correspondence: Hélène Sanfaçon helene.sanfacon@agr.gc.ca

This article was submitted to Virology, a section of the journal Frontiers in Microbiology

 12 09 2017 2017 8 1762 21 08 2017 30 08 2017 Copyright © 2017 Mann, Walker and Sanfaçon. 2017 Mann, Walker and Sanfaçon

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 A corrigendum on Identification of Cleavage Sites Recognized by the 3C-Like Cysteine Protease within the Two Polyproteins of Strawberry Mottle Virus by Mann, K. S., Walker, M. C., and Sanfaçon, H. (2017). Front. Microbiol. 8:745. doi: 10.3389/fmicb.2017.00745 proteolytic processing viral proteases plant virus cleavage site specificity 3C protease picornavirales secoviridae in vitro translation Agriculture and Agri-Food Canada10.13039/501100000040

In the original article, there were mistakes in Table 2 as published. Several listed cleavage sites were derived from virus isolates that did not correspond to the accession numbers provided in the Materials and Methods Section. In addition, the sequence listed for the DMaV NTB-VPg cleavage site was incorrect and showed the sequence for the VPg-Pro cleavage site instead. Corrections to the SMoV MP-CP cleavage site, BRNV MP-CP cleavage site, and DMaV X1-X2, NTB-VPg, and Pro-Pol cleavage sites have been made. Please note that this correction does not change amino acids at conserved positions (highlighted in red or green in the Table). The corrected Table 2 appears below. The authors apologize for this error and state that this does not change the scientific conclusions of the article in any way.

Alignment of potential cleavage sites for members of the family Secoviridae.

SMoV BRNV CLVA DMaV
P1 SITES
X1-X2 AQCVEQ/GG IGLEQE/GF EHETCQ/GL TEEELQ/GL
X2-NTB CPAYEQ/SS DVPLSE/GA ADVAAQ/SG EPMMLQ/AG
NTB-VPg EVATEQ/GG LAFTSE/GG SSSLAQ/GT TESELQ/GV
VPg-Pro VRAYEQ/GA IKPYSQ/GG RAFSAQ/GE RGFQLQ/GG
Pro-Pol EVAVQQ/GM GKFYQQ/GD PVIVAQ/GP PADELQ/SE
P2 SITES
MP-CP TRAYEE/GXF DDFVEE/GG GDAAAQ/GD LNDSLE/GD

Amino acids highlighted in red represents highly conserved positions. Amino acids highlighted in green represent alternative amino acids found at the −4, −2, −1, or +1 positions. SMoV, Strawberry mottle virus; BRNV, black raspberry necrosis virus; CLVA, chocolate lily virus A; DMaV, dioscorea mosaic-associated virus; NTB, nucleoside triphosphate binding protein; VPg, viral genome-linked protein; Pro, protease; Pol, polymerase; X1 and X2, unknown; MP, movement protein; CP, capsid protein.

 Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.