scholarly journals Mutagenesis Mapping of RNA Structures within the Foot-and-Mouth Disease Virus Genome Reveals Functional Elements Localized in the Polymerase (3D pol )-Encoding Region

mSphere ◽  
2021 ◽  
Author(s):  
Lidia Lasecka-Dykes ◽  
Fiona Tulloch ◽  
Peter Simmonds ◽  
Garry A. Luke ◽  
Paolo Ribeca ◽  
...  
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Virus Genome ◽  
Mouth Disease ◽  
Rna Structures ◽  
Nonstructural Proteins ◽  
Functional Elements ◽  
Subgenomic Replicon ◽  
Mouth Disease Virus ◽  
Foot And Mouth

Some RNA structures formed by the genomes of RNA viruses are critical for viral replication. Our study shows that of 46 conserved RNA structures located within the regions of the foot-and-mouth disease virus (FMDV) genome that encode the nonstructural proteins, only 3 are essential for replication of an FMDV subgenomic replicon.

scholarly journals Synthetic RNAs Mimicking Structural Domains in the Foot-and-Mouth Disease Virus Genome Elicit a Broad Innate Immune Response in Porcine Cells Triggered by RIG-I and TLR Activation

Viruses ◽  
2015 ◽  
Vol 7 (7) ◽  
pp. 3954-3973 ◽  
Author(s):  
Belén Borrego ◽  
Miguel Rodríguez-Pulido ◽  
Concepción Revilla ◽  
Belén Álvarez ◽  
Francisco Sobrino ◽  
...  
Keyword(s):  
Immune Response ◽  
Disease Virus ◽  
Innate Immune Response ◽  
Foot And Mouth Disease ◽  
Virus Genome ◽  
Mouth Disease ◽  
Innate Immune ◽  
Structural Domains ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Inhibition of the foot-and-mouth disease virus subgenomic replicon by RNA aptamers

2014 ◽  
Vol 95 (12) ◽  
pp. 2649-2657 ◽  
Author(s):  
Sophie Forrest ◽  
Zoe Lear ◽  
Morgan R. Herod ◽  
Martin Ryan ◽  
David J. Rowlands ◽  
...  
Keyword(s):  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Rna Aptamers ◽  
Gfp Expression ◽  
Subgenomic Replicon ◽  
Replication Complex ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Dose Dependent

We have previously documented the inhibitory activity of RNA aptamers to the RNA-dependent RNA polymerase of foot-and-mouth disease virus (3Dpol). Here we report their modification and use with a subgenomic replicon incorporating GFP (pGFP-PAC replicon), allowing replication to be monitored and quantified in real-time. GFP expression in transfected BHK-21 cells reached a maximum at approximately 8 h post-transfection, at which time change in morphology of the cells was consistent with a virus-induced cytopathic effect. However, transfection of replicon-bearing cells with a 3Dpol aptamer RNA resulted in inhibition of GFP expression and maintenance of normal cell morphology, whereas a control aptamer RNA had little effect. The inhibition was correlated with a reduction in 3Dpol (detected by immunoblotting) and shown to be dose dependent. The 3Dpol aptamers appeared to be more effective than 2′-C-methylcytidine (2′CMC). Aptamers to components of the replication complex are therefore useful molecular tools for studying viral replication and also have potential as diagnostic molecules in the future.

scholarly journals Evidence for the role of His-142 of protein 1C in the acid-induced disassembly of foot-and-mouth disease virus capsids

1999 ◽  
Vol 80 (8) ◽  
pp. 1911-1918 ◽  
Author(s):  
Fiona M. Ellard ◽  
Jeff Drew ◽  
Wendy E. Blakemore ◽  
David I. Stuart ◽  
Andrew M. Q. King
Keyword(s):  
Disease Virus ◽  
Expression System ◽  
Foot And Mouth Disease ◽  
Dipole Interaction ◽  
Virus Genome ◽  
Mouth Disease ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Acidic Conditions ◽  
Α Helix

Foot-and-mouth disease virus (FMDV) capsids are inherently labile under mildly acidic conditions, dissociating to pentamers at pH values in the region of 6·5, with the release of protein 1A and the viral RNA. This acid-induced disassembly is thought to be required for the entry of the virus genome into the host cell. Previous work has highlighted a histidine–α-helix charge-dipole interaction at the twofold axes of symmetry between pentamers and has suggested that this interaction plays a role in acid-induced disassembly. The validity of this theory has now been tested by converting the implicated residue, His-142 of protein 1C, to Arg, Phe and Asp. The effects of such changes were studied by using a previously described vaccinia virus expression system, in which synthesis and processing of FMDV capsid proteins results in the self-assembly of capsids. In agreement with the histidine–α-helix charge-dipole theory, assembly in the arginine mutant was found to be greatly reduced, while capsids of the aspartic acid mutant were considerably more stable under acidic conditions than the wild-type. Aberrant but acid-stable complexes were obtained in the phenylalanine mutant.

scholarly journals Inter-laboratory comparison of 2 ELISA kits used for foot-and-mouth disease virus nonstructural protein serology

2020 ◽  
Vol 32 (6) ◽  
pp. 933-937
Author(s):  
Clare F. J. Browning ◽  
Antonello Di Nardo ◽  
Lissie Henry ◽  
Tim Pollard ◽  
Lynne Hendry ◽  
...  
Keyword(s):  
Disease Virus ◽  
Disease Surveillance ◽  
Nonstructural Protein ◽  
Foot And Mouth Disease ◽  
Screen Test ◽  
Mouth Disease ◽  
Nonstructural Proteins ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Thermo Fisher Scientific

Serologic assays used to detect antibodies to nonstructural proteins (NSPs) of foot-and-mouth disease virus (FMDV) are used for disease surveillance in endemic countries, and are essential to providing evidence for freedom of the disease with or without vaccination and to recover the free status of a country after an outbreak. In a 5-site inter-laboratory study, we compared the performance of 2 commercial NSP ELISA kits (ID Screen FMD NSP ELISA single day [short] and overnight protocols, ID.Vet; PrioCHECK FMDV NS antibody ELISA, Thermo Fisher Scientific). The overall concordance between the PrioCHECK and ID Screen test was 93.8% (95% CI: 92.0–95.2%) and 94.8% (95% CI: 93.1–96.1%) for the overnight and short ID Screen incubation protocols, respectively. Our results indicate that the assays (including the 2 different formats of the ID Screen test) can be used interchangeably in post-outbreak serosurveillance.

scholarly journals Identification of T-Cell Epitopes in Nonstructural Proteins of Foot-and-Mouth Disease Virus

2001 ◽  
Vol 75 (7) ◽  
pp. 3164-3174 ◽  
Author(s):  
E. Blanco ◽  
M. Garcia-Briones ◽  
A. Sanz-Parra ◽  
P. Gomes ◽  
E. De Oliveira ◽  
...  
Keyword(s):  
T Cell ◽  
Disease Virus ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
T Cell Epitopes ◽  
Nonstructural Proteins ◽  
Mouth Disease Virus ◽  
Foot And Mouth

scholarly journals Bovine Serum Panel for Evaluating Foot-and-Mouth Disease Virus Nonstructural Protein Antibody Tests

2007 ◽  
Vol 19 (5) ◽  
pp. 539-544 ◽  
Author(s):  
Satya Parida ◽  
Lucy Fleming ◽  
Debi Gibson ◽  
Pip A. Hamblin ◽  
Santina Grazioli ◽  
...  
Keyword(s):  
Disease Virus ◽  
Nonstructural Protein ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Infected Cattle ◽  
Nonstructural Proteins ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Contact Exposure ◽  
Antibody Tests

A panel of 36 sera has been assembled from experimental cattle that had been infected by inoculation or contact exposure with 4 serotypes of foot-and-mouth disease virus (FMDV) with or without prior vaccination. Virus replication and persistence had been characterized in all of the animals. The proportion of the sera scored positive by 5 tests for antibodies to the nonstructural proteins of FMDV varied, suggesting that the panel can discriminate between the sensitivity with which such tests are able to identify infected cattle. Use of this panel will help in assessment of new tests and quality control of existing methods.

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