scholarly journals Subcellular Distribution of the Foot-and-Mouth Disease Virus 3A Protein in Cells Infected with Viruses Encoding Wild-Type and Bovine-Attenuated Forms of 3A

Virology ◽  
2001 ◽  
Vol 287 (1) ◽  
pp. 151-162 ◽  
Author(s):  
Vivian K. O'Donnell ◽  
Juan M. Pacheco ◽  
Tina M. Henry ◽  
Peter W. Mason
Keyword(s):  
Disease Virus ◽  
Subcellular Distribution ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Wild Type ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
In Cells

scholarly journals Identification and Characterization of a cis-Acting Replication Element (cre) Adjacent to the Internal Ribosome Entry Site of Foot-and-Mouth Disease Virus

2002 ◽  
Vol 76 (19) ◽  
pp. 9686-9694 ◽  
Author(s):  
Peter W. Mason ◽  
Svetlana V. Bezborodova ◽  
Tina M. Henry
Keyword(s):  
Disease Virus ◽  
Internal Ribosome Entry Site ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Wild Type ◽  
Coding Region ◽  
Entry Site ◽  
Internal Ribosome Entry ◽  
Mouth Disease Virus ◽  
Foot And Mouth

ABSTRACT Over the last few years, an essential RNA structure known as the cis-acting replicative element (cre) has been identified within the protein-coding region of several picornaviruses. The cre, a stem-loop structure containing a conserved AAACA motif, functions as a template for addition of U residues to the protein primer 3B. By surveying the genomes of representatives of several serotypes of foot-and-mouth disease virus (FMDV), we discovered a putative cre in the 5′ untranslated region of the genome (contiguous with the internal ribosome entry site [IRES]). To confirm the role of this putative cre in replication, we tested the importance of the AAACA motif and base pairing in the stem in FMDV genome replication. To this end, cre mutations were cloned into an FMDV replicon and into synthetic viral genomes. Analyses of the properties of these replicons and genomes revealed the following. (i) Mutations in the AAACA motif severely reduced replication, and all viruses recovered from genomes containing mutated AAACA sequences had reverted to the wild-type sequence. (ii) Mutations in the stem region showed that the ability to form this base-paired structure was important for replication. Although the cre was contiguous with the IRES, the mutations we created did not significantly reduce IRES-mediated translation in vivo. Finally, the position of the cre at the 5′ end of the genome was shown not to be critical for replication, since functional replicons and viruses lacking the 5′ cre could be obtained if a wild-type cre was added to the genome following the 3Dpol coding region. Taken together, these results support the importance of the cre in replication and demonstrate that the activity of this essential element does not require localization within the polyprotein-encoding region of the genome.

scholarly journals Pathogenesis of wild-type and leaderless foot-and-mouth disease virus in cattle.

1996 ◽  
Vol 70 (8) ◽  
pp. 5638-5641 ◽  
Author(s):  
C C Brown ◽  
M E Piccone ◽  
P W Mason ◽  
T S McKenna ◽  
M J Grubman
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Wild Type ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Identification of RNA Helicase A as a New Host Factor in the Replication Cycle of Foot-and-Mouth Disease Virus

2009 ◽  
Vol 83 (21) ◽  
pp. 11356-11366 ◽  
Author(s):  
Paul Lawrence ◽  
Elizabeth Rieder
Keyword(s):  
Disease Virus ◽  
Subcellular Distribution ◽  
Foot And Mouth Disease ◽  
Rna Helicase ◽  
Mouth Disease ◽  
Rna Helicase A ◽  
New Host ◽  
Nontranslated Region ◽  
Mouth Disease Virus ◽  
Foot And Mouth

ABSTRACT Foot-and-mouth disease virus (FMDV), as with other RNA viruses, recruits various host cell factors to assist in the translation and replication of the virus genome. In this study, we investigated the role of RNA helicase A (RHA) in the life cycle of FMDV. Immunofluorescent microscopy (IFM) showed a change in the subcellular distribution of RHA from the nucleus to the cytoplasm in FMDV-infected cells as infection progressed. Unlike nuclear RHA, the RHA detected in the cytoplasm reacted with an antibody that recognizes only the nonmethylated form of RHA. In contrast to alterations in the subcellular distribution of nuclear factors observed during infection with the related cardioviruses, cytoplasmic accumulation of RHA did not require the activity of the FMDV leader protein. Using IFM, we have found cytoplasmic RHA in proximity to the viral 2C and 3A proteins, which promotes the assembly of the replication complexes, as well as cellular poly(A) binding protein (PABP). Coimmunoprecipitation assays confirmed that these proteins are complexed with RHA. We have also identified a novel interaction between RHA and the S fragment in the FMDV 5′ nontranslated region. Moreover, a reduction in the expression of RHA, using RHA-specific small interfering RNA constructs, inhibited FMDV replication. These results indicate that RHA plays an essential role in the replication of FMDV and potentially other picornaviruses through ribonucleoprotein complex formation at the 5′ end of the genome and by interactions with 2C, 3A, and PABP.

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