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Identification of residues within the African swine fever virus DP71L protein required for dephosphorylation of translation initiation factor eIF2α and inhibiting activation of proapoptotic CHOP

Goodbourn, SE; moon, A; Barber, C; Dixon, L; Netherton, C; Goatley, L (2017) Identification of residues within the African swine fever virus DP71L protein required for dephosphorylation of translation initiation factor eIF2α and inhibiting activation of proapoptotic CHOP. VIROLOGY, 504. pp. 107-113. ISSN 0042-6822
SGUL Authors: Goodbourn, Stephen Edward

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Abstract

The African swine fever virus DP71L protein recruits protein phosphatase 1 (PP1) to dephosphorylate the translation initiation factor 2α (eIF2α) and avoid shut-off of global protein synthesis and downstream activation of the pro-apoptotic factor CHOP. Residues V16 and F18A were critical for binding of DP71L to PP1. Mutation of this PP1 binding motif or deletion of residues between 52 and 66 reduced the ability of DP71L to cause dephosphorylation of eIF2α and inhibit CHOP induction. The residues LSAVL, between 57 and 61, were also required. PP1 was co-precipitated with wild type DP71L and the mutant lacking residues 52- 66 or the LSAVL motif, but not with the PP1 binding motif mutant. The residues in the LSAVL motif play a critical role in DP71L function but do not interfere with binding to PP1. Instead we propose these residues are important for DP71L binding to eIF2α.

Item Type: Article
Additional Information: © 2017 The Author(s). Published by Elsevier Inc. This is an open access article under the CC BY license (http://creativecommons.org/licenses/BY/4.0/).
Keywords: Virology, 06 Biological Sciences, 11 Medical And Health Sciences, 07 Agricultural And Veterinary Sciences
SGUL Research Institute / Research Centre: Academic Structure > Infection and Immunity Research Institute (INII)
Journal or Publication Title: VIROLOGY
ISSN: 0042-6822
Dates:
DateEvent
3 February 2017Accepted
9 February 2017Published Online
1 April 2017Published
Projects:
Project IDFunderFunder ID
BBS/E/I/00001714Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
BB/P005195/1Biotechnology and Biological Sciences Research Councilhttp://dx.doi.org/10.13039/501100000268
URI: https://openaccess.sgul.ac.uk/id/eprint/108584

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