Recruitment of host translation initiation factor eIF4G by the Vaccinia Virus ssDNA-binding protein I3

Izabela Zaborowska; Kerstin Kellner; Michael Henry; Paula Meleady; Derek Walsh

doi:10.1016/j.virol.2011.12.022

Recruitment of host translation initiation factor eIF4G by the Vaccinia Virus ssDNA-binding protein I3

Izabela Zaborowska, Kerstin Kellner, Michael Henry, Paula Meleady, Derek Walsh^*

^*Corresponding author for this work

Microbiology-Immunology

Research output: Contribution to journal › Article › peer-review

22 Scopus citations

Abstract

Poxviruses are large double-stranded DNA viruses that replicate exclusively in the cytoplasm of infected cells within discrete compartments termed viral factories. Recent work has shown that the prototypical poxvirus, Vaccinia Virus (VacV) sequesters components of the eukaryotic translation initiation complex eIF4F within viral factories while also stimulating formation of eIF4F complexes. However, the forces that govern these events remain unknown. Here, we show that maximal eIF4F formation requires viral DNA replication and the formation of viral factories, suggesting that sequestration functions to promote eIF4F assembly, and identify the ssDNA-binding protein, I3 as a viral factor that interacts and co-localizes with the eIF4F scaffold protein, eIF4G. Although it did not adversely affect host or viral protein synthesis, I3 specifically mediated the binding of eIF4G to ssDNA. Combined, our findings offer an explanation for the specific pattern and temporal process of eIF4G redistribution and eIF4F complex assembly within VacV-infected cells.

Original language	English (US)
Pages (from-to)	11-22
Number of pages	12
Journal	Virology
Volume	425
Issue number	1
DOIs	https://doi.org/10.1016/j.virol.2011.12.022
State	Published - Mar 30 2012

Funding

We thank Ian Mohr, Stewart Shuman, Simon Morley, David Evans, Nicole Favis and Jacomine Krijnse-Locker for kindly providing us with reagents. We would also like to thank Bernard Moss and Arban Domi for their advice and kind gift of the Vac-BAC/λ system used in our attempt to generate an I3L mutant. This work was supported by grants from the Health Research Board ( RP/2007/52 ) to D.W. and from Science Foundation Ireland ( 07 IN.1 B1323 ).

Keywords

EIF4F
EIF4G
I3
Poxvirus
Translation initiation

ASJC Scopus subject areas

Virology

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10.1016/j.virol.2011.12.022

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title = "Recruitment of host translation initiation factor eIF4G by the Vaccinia Virus ssDNA-binding protein I3",

abstract = "Poxviruses are large double-stranded DNA viruses that replicate exclusively in the cytoplasm of infected cells within discrete compartments termed viral factories. Recent work has shown that the prototypical poxvirus, Vaccinia Virus (VacV) sequesters components of the eukaryotic translation initiation complex eIF4F within viral factories while also stimulating formation of eIF4F complexes. However, the forces that govern these events remain unknown. Here, we show that maximal eIF4F formation requires viral DNA replication and the formation of viral factories, suggesting that sequestration functions to promote eIF4F assembly, and identify the ssDNA-binding protein, I3 as a viral factor that interacts and co-localizes with the eIF4F scaffold protein, eIF4G. Although it did not adversely affect host or viral protein synthesis, I3 specifically mediated the binding of eIF4G to ssDNA. Combined, our findings offer an explanation for the specific pattern and temporal process of eIF4G redistribution and eIF4F complex assembly within VacV-infected cells.",

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N2 - Poxviruses are large double-stranded DNA viruses that replicate exclusively in the cytoplasm of infected cells within discrete compartments termed viral factories. Recent work has shown that the prototypical poxvirus, Vaccinia Virus (VacV) sequesters components of the eukaryotic translation initiation complex eIF4F within viral factories while also stimulating formation of eIF4F complexes. However, the forces that govern these events remain unknown. Here, we show that maximal eIF4F formation requires viral DNA replication and the formation of viral factories, suggesting that sequestration functions to promote eIF4F assembly, and identify the ssDNA-binding protein, I3 as a viral factor that interacts and co-localizes with the eIF4F scaffold protein, eIF4G. Although it did not adversely affect host or viral protein synthesis, I3 specifically mediated the binding of eIF4G to ssDNA. Combined, our findings offer an explanation for the specific pattern and temporal process of eIF4G redistribution and eIF4F complex assembly within VacV-infected cells.

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Recruitment of host translation initiation factor eIF4G by the Vaccinia Virus ssDNA-binding protein I3

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