The N-terminal region (VP4) of the foot-and-mouth disease capsid precursor (P1-2A) is not required during its synthesis to allow subsequent processing by the 3C protease

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The N-terminal region (VP4) of the foot-and-mouth disease capsid precursor (P1-2A) is not required during its synthesis to allow subsequent processing by the 3C protease. / Kristensen, Thea; Normann, Preben; Belsham, Graham J.

In: Virology, Vol. 570, 2022, p. 29-34.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Kristensen, T, Normann, P & Belsham, GJ 2022, 'The N-terminal region (VP4) of the foot-and-mouth disease capsid precursor (P1-2A) is not required during its synthesis to allow subsequent processing by the 3C protease', Virology, vol. 570, pp. 29-34. https://doi.org/10.1016/j.virol.2022.03.006

APA

Kristensen, T., Normann, P., & Belsham, G. J. (2022). The N-terminal region (VP4) of the foot-and-mouth disease capsid precursor (P1-2A) is not required during its synthesis to allow subsequent processing by the 3C protease. Virology, 570, 29-34. https://doi.org/10.1016/j.virol.2022.03.006

Vancouver

Kristensen T, Normann P, Belsham GJ. The N-terminal region (VP4) of the foot-and-mouth disease capsid precursor (P1-2A) is not required during its synthesis to allow subsequent processing by the 3C protease. Virology. 2022;570:29-34. https://doi.org/10.1016/j.virol.2022.03.006

Author

Kristensen, Thea ; Normann, Preben ; Belsham, Graham J. / The N-terminal region (VP4) of the foot-and-mouth disease capsid precursor (P1-2A) is not required during its synthesis to allow subsequent processing by the 3C protease. In: Virology. 2022 ; Vol. 570. pp. 29-34.

Bibtex

@article{42e5a5632b044a709f2cee606b16ad0c,
title = "The N-terminal region (VP4) of the foot-and-mouth disease capsid precursor (P1-2A) is not required during its synthesis to allow subsequent processing by the 3C protease",
abstract = "The capsid precursor (P1-2A) of foot-and-mouth disease virus is processed by the 3C protease (3Cpro) to VP0, VP3 and VP1 plus 2A. During capsid assembly, the VP0 is cleaved to VP4 plus VP2. Single amino acid changes in a conserved motif (YCPRP) near the C-terminus of VP1 can block processing of the capsid precursor by the 3Cpro, although the cleavage sites are located hundreds of amino acids distant from this motif, presumably due to misfolding. In contrast, we show here that the absence of the VP4 sequence during the synthesis of the capsid precursor does not affect its subsequent processing. Cleavage of this truncated precursor by 3Cpro at the VP3/VP1 and VP2/VP3 junctions occurred efficiently. Thus, in contrast to the presence of the YCPRP motif in VP1, there are no critical motifs near the N-terminus of the precursor, within VP4, required for correct cleavage by 3Cpro.",
keywords = "Capsid assembly, Chaperone, Myristoylation, Picornavirus, Polyprotein processing",
author = "Thea Kristensen and Preben Normann and Belsham, {Graham J.}",
note = "Publisher Copyright: {\textcopyright} 2022 The Authors",
year = "2022",
doi = "10.1016/j.virol.2022.03.006",
language = "English",
volume = "570",
pages = "29--34",
journal = "Virology",
issn = "0042-6822",
publisher = "Academic Press",

}

RIS

TY - JOUR

T1 - The N-terminal region (VP4) of the foot-and-mouth disease capsid precursor (P1-2A) is not required during its synthesis to allow subsequent processing by the 3C protease

AU - Kristensen, Thea

AU - Normann, Preben

AU - Belsham, Graham J.

N1 - Publisher Copyright: © 2022 The Authors

PY - 2022

Y1 - 2022

N2 - The capsid precursor (P1-2A) of foot-and-mouth disease virus is processed by the 3C protease (3Cpro) to VP0, VP3 and VP1 plus 2A. During capsid assembly, the VP0 is cleaved to VP4 plus VP2. Single amino acid changes in a conserved motif (YCPRP) near the C-terminus of VP1 can block processing of the capsid precursor by the 3Cpro, although the cleavage sites are located hundreds of amino acids distant from this motif, presumably due to misfolding. In contrast, we show here that the absence of the VP4 sequence during the synthesis of the capsid precursor does not affect its subsequent processing. Cleavage of this truncated precursor by 3Cpro at the VP3/VP1 and VP2/VP3 junctions occurred efficiently. Thus, in contrast to the presence of the YCPRP motif in VP1, there are no critical motifs near the N-terminus of the precursor, within VP4, required for correct cleavage by 3Cpro.

AB - The capsid precursor (P1-2A) of foot-and-mouth disease virus is processed by the 3C protease (3Cpro) to VP0, VP3 and VP1 plus 2A. During capsid assembly, the VP0 is cleaved to VP4 plus VP2. Single amino acid changes in a conserved motif (YCPRP) near the C-terminus of VP1 can block processing of the capsid precursor by the 3Cpro, although the cleavage sites are located hundreds of amino acids distant from this motif, presumably due to misfolding. In contrast, we show here that the absence of the VP4 sequence during the synthesis of the capsid precursor does not affect its subsequent processing. Cleavage of this truncated precursor by 3Cpro at the VP3/VP1 and VP2/VP3 junctions occurred efficiently. Thus, in contrast to the presence of the YCPRP motif in VP1, there are no critical motifs near the N-terminus of the precursor, within VP4, required for correct cleavage by 3Cpro.

KW - Capsid assembly

KW - Chaperone

KW - Myristoylation

KW - Picornavirus

KW - Polyprotein processing

U2 - 10.1016/j.virol.2022.03.006

DO - 10.1016/j.virol.2022.03.006

M3 - Journal article

C2 - 35364457

AN - SCOPUS:85127190678

VL - 570

SP - 29

EP - 34

JO - Virology

JF - Virology

SN - 0042-6822

ER -

ID: 307374985