HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Erratum Erratum (v85,p3817) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Strong, R. Articles by Belsham, G. J. Search for Related Content PubMed PubMed Citation Articles by Strong, R. Articles by Belsham, G. J. Agricola Articles by Strong, R. Articles by Belsham, G. J.

Sequential modification of translation initiation factor eIF4GI by two different foot-and-mouth disease virus proteases within infected baby hamster kidney cells: identification of the 3C^pro cleavage site

Institute for Animal Health, Pirbright, Woking, Surrey GU24 0NF, UK

Correspondence
Graham J. Belsham
graham.belsham{at}bbsrc.ac.uk

Infection of cells by foot-and-mouth disease virus (FMDV) causes the rapid inhibition of cellular cap-dependent protein synthesis that results from cleavage of the translation initiation factor eIF4G, a component of the cap-binding complex eIF4F. Two FMDV proteins, the leader (L) and 3C proteases, have been shown individually to induce cleavage of eIF4GI at distinct sites within baby hamster kidney (BHK) cells. Here, sequential cleavage of eIF4GI by the L and 3C proteases was demonstrated in FMDV-infected BHK cells. The FMDV 3C cleavage site within hamster eIF4GI was localized to a small region (about 40 aa) of the protein, between the sites cleaved by the poliovirus 2A protease and the human immunodeficiency virus type 2 protease. Human eIF4GI was found to be resistant to the action of the FMDV 3C protease. On the basis of amino acid sequence alignments, it was predicted and then verified that substitution of a single amino acid residue within this region of human eIF4GI conferred sensitivity to cleavage by the FMDV 3C protease within cells. Full-length eIF4GI and both forms of the C-terminal cleavage product must be capable of supporting the activity of the FMDV internal ribosome entry site in directing translation initiation.

The GenBank/EMBL/DDBJ accession numbers for the partial eIF4GI cDNA sequences reported in this paper are AJ746218 (ovine), AJ746219 (bovine), AJ746220 (hamster), AJ746221 (equine), AJ746222 (murine), AJ746223 (porcine) and AJ746224 (rabbit).

This article has been cited by other articles:

				T. de los Santos, F. Diaz-San Segundo, J. Zhu, M. Koster, C. C. A. Dias, and M. J. Grubman A Conserved Domain in the Leader Proteinase of Foot-and-Mouth Disease Virus Is Required for Proper Subcellular Localization and Function J. Virol., February 15, 2009; 83(4): 1800 - 1810. [Abstract] [Full Text] [PDF]

				E. Martinez-Salas, A. Pacheco, P. Serrano, and N. Fernandez New insights into internal ribosome entry site elements relevant for viral gene expression J. Gen. Virol., March 1, 2008; 89(3): 611 - 626. [Abstract] [Full Text] [PDF]

				C. Hohle, A. Karger, P. Konig, K. Giesow, and G. M. Keil High-level expression of biologically active bovine alpha interferon by Bovine herpesvirus 1 interferes only marginally with recombinant virus replication in vitro J. Gen. Virol., October 1, 2005; 86(10): 2685 - 2695. [Abstract] [Full Text] [PDF]