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Journal of Virology, November 1998, p. 8813-8819, Vol. 72, No. 11
BBSRC Institute for Animal Health, Pirbright,
Woking, Surrey GU24 ONF, United Kingdom
Received 5 May 1998/Accepted 24 July 1998
The role of the cap-binding complex, eIF4F, in the translation of
vaccinia virus mRNAs has been analyzed within infected cells. Plasmid
DNAs, which express dicistronic mRNAs containing a picornavirus internal ribosome entry site, produced within vaccinia virus-infected cells both
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Vaccinia Virus Protein Synthesis Has a Low
Requirement for the Intact Translation Initiation Factor eIF4F, the
Cap-Binding Complex, within Infected Cells
-glucuronidase and a cell surface-targeted single-chain antibody (sFv). Cells expressing sFv were selected from nonexpressing cells, enabling analysis of protein synthesis specifically within the
transfected cells. Coexpression of poliovirus 2A or foot-and-mouth disease virus Lb proteases, which cleaved translation initiation factor
eIF4G, greatly inhibited cap-dependent protein (
-glucuronidase) synthesis. Under these conditions, internal ribosome entry
site-directed expression of sFv continued and cell selection was
maintained. Furthermore, vaccinia virus protein synthesis persisted in
the selected cells containing cleaved eIF4G. Thus, late vaccinia virus protein synthesis has a low requirement for the intact cap-binding complex eIF4F. This may be attributed to the short unstructured 5'
noncoding regions of the vaccinia virus mRNAs, possibly aided by the
presence of poly(A) at both 5' and 3' termini.
*
Corresponding author. Mailing address: BBSRC Institute
for Animal Health, Pirbright Laboratory, Ash Road, Pirbright, Woking, Surrey GU24 ONF, United Kingdom. Phone: 44-1483 232441. Fax: 44-1483 232448. E-mail: graham.belsham{at}bbsrc.ac.uk.
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