Proteomics

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African swine fever virus ubiquitinconjugating enzyme interacts with host translation machinery to regulate the host protein synthesis


ABSTRACT: African Swine Fever virus (ASFV) causes one of the most relevant emerging diseases affecting swine, now extended through three continents. The virus has a large coding capacity to deploy an arsenal of molecules antagonizing the host functions. In the present work, we have studied the only known E2 viral-conjugating enzyme, UBCv1 that is encoded by the I215L gene of ASFV. SILAC quantitative proteomics was used toidentify and characterize novel UBCv1-host interactors. The analysis revealed interaction with the 40S ribosomal protein RPS23, the cap-dependent translation machinery initiation factor eIF4E, and the E3 ubiquitin ligase Cullin 4B. Our data show that during ASFV infection, UBCv1 was able to bind to eIF4E, independent from the cap-dependent complex. Our results provide novel insights into the function of the viral UBCv1 in hijacking cellular components that impact the mTORC signalling pathway, the regulation of the host translation machinery, and the cellular protein expression during the ASFV lifecycle. The people involved in this project are: Lucia Barrado-Gil, Covadonga Alonso and Carlos Maluquer de Motes.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: Carlos Maluquer de Motes  

LAB HEAD: Carlos Maluquer de Motes

PROVIDER: PXD023086 | Pride | 2020-12-14

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
290617_Rep1.raw Raw
290617_Rep2.raw Raw
290617_Rep3.raw Raw
UBCv1SILACData.xlsx Xlsx
checksum.txt Txt
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