A 65 S particle containing viral protein in cells infected with foot-and-mouth disease virus

Foot-and-mouth disease, caused by foot-and-mouth disease virus (FMDV), is one of the most dangerous diseases of cloven-hoofed animals and is a constant threat to the dairy and beef industries in the Middle East and other regions of the world, despite intensive vaccination programmes. In this work, the ability of specific small interfering (si)RNAs to inhibit virus replication in BHK-21 cells was examined. By using bioinformatic computer programs, all FMDV sequences in public-domain databases were analysed. The analysis revealed three regions of at least 22 bp with 100 % identity in all FMDV entries. From these sequences, three specific siRNA molecules were prepared and used to test the ability of siRNAs to inhibit virus replication. By using real-time quantitative PCR to measure the amount of viral RNA in infected cells, it was shown that virus replication was inhibited in cells that were transfected with siRNAs. When viral titres were examined, 100 % inhibition of growth could be demonstrated in cells transfected with a mixture of all three anti-FMDV siRNAs, compared with control cells transfected with anti-LacZ siRNA.

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Virus-resistant pigs might help to stem next outbreak

eLife ◽

10.7554/elife.09790 ◽

2015 ◽

Vol 4 ◽

Cited By ~ 1

Author(s):

Lisbeth Ramirez-Carvajal ◽

Luis L Rodriguez

Keyword(s):

Disease Virus ◽

Viral Protein ◽

Foot And Mouth Disease ◽

Mouth Disease ◽

Mouth Disease Virus ◽

Foot And Mouth

By genetically engineering pigs to degrade a crucial viral protein, livestock can be made less susceptible to foot and mouth disease virus.

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The DEAD-Box RNA Helicase DDX1 Interacts with the Viral Protein 3D and Inhibits Foot-and-Mouth Disease Virus Replication

Virologica Sinica ◽

10.1007/s12250-019-00148-7 ◽

2019 ◽

Vol 34 (6) ◽

pp. 610-617 ◽

Cited By ~ 7

Author(s):

Qiao Xue ◽

Huisheng Liu ◽

Qiaoying Zeng ◽

Haixue Zheng ◽

Qinghong Xue ◽

...

Keyword(s):

Disease Virus ◽

Virus Replication ◽

Viral Protein ◽

Foot And Mouth Disease ◽

Rna Helicase ◽

Mouth Disease ◽

Dead Box ◽

Mouth Disease Virus ◽

Foot And Mouth ◽

The Dead

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A Conserved Domain in the Leader Proteinase of Foot-and-Mouth Disease Virus Is Required for Proper Subcellular Localization and Function

Journal of Virology ◽

10.1128/jvi.02112-08 ◽

2008 ◽

Vol 83 (4) ◽

pp. 1800-1810 ◽

Cited By ~ 53

Author(s):

Teresa de los Santos ◽

Fayna Diaz-San Segundo ◽

James Zhu ◽

Marla Koster ◽

Camila C. A. Dias ◽

...

Keyword(s):

Disease Virus ◽

Double Mutant ◽

Foot And Mouth Disease ◽

Mrna Translation ◽

Mouth Disease ◽

Mutant Virus ◽

Mouth Disease Virus ◽

Foot And Mouth ◽

Infected Cells ◽

In Cells

ABSTRACT The leader proteinase (Lpro) of foot-and-mouth disease virus (FMDV) is involved in antagonizing the innate immune response by blocking the expression of interferon (IFN) and by reducing the immediate-early induction of IFN-β mRNA and IFN-stimulated genes. In addition to its role in shutting off cap-dependent host mRNA translation, Lpro is associated with the degradation of the p65/RelA subunit of nuclear factor κB (NF-κB). Bioinformatics analysis suggests that Lpro contains a SAP (for SAF-A/B, Acinus, and PIAS) domain, a protein structure associated in some cases with the nuclear retention of molecules involved in transcriptional control. We have introduced a single or a double mutation in conserved amino acid residues contained within this domain of Lpro. Although three stable mutant viruses were obtained, only the double mutant displayed an attenuated phenotype in cell culture. Indirect immunofluorescence analysis showed that Lpro subcellular distribution is altered in cells infected with the double mutant virus. Interestingly, nuclear p65/RelA staining disappeared from wild-type (WT) FMDV-infected cells but not from double mutant virus-infected cells. Consistent with these results, NF-κB-dependent transcription was not inhibited in cells infected with double mutant virus in contrast to cells infected with WT virus. However, degradation of the translation initiation factor eIF-4G was very similar for both the WT and the double mutant viruses. Since Lpro catalytic activity was demonstrated to be a requirement for p65/RelA degradation, our results indicate that mutation of the SAP domain reveals a novel separation-of-function activity for FMDV Lpro.

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High resolution surface structure of foot-and-mouth disease virus

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100082741 ◽

1978 ◽

Vol 36 (2) ◽

pp. 376-377

Author(s):

S. S. Breese ◽

H. L. Bachrach

Keyword(s):

Electron Microscopy ◽

High Resolution ◽

Surface Structure ◽

Disease Virus ◽

Potassium Phosphate ◽

Foot And Mouth Disease ◽

Mouth Disease ◽

Physical Measurements ◽

Mouth Disease Virus ◽

Foot And Mouth

Models for the structure of foot-and-mouth disease virus (FMDV) have been proposed from chemical and physical measurements (Brown, et al., 1970; Talbot and Brown, 1972; Strohmaier and Adam, 1976) and from rotational image-enhancement electron microscopy (Breese, et al., 1965). In this report we examine the surface structure of FMDV particles by high resolution electron microscopy and compare it with that of particles in which the outermost capsid protein VP3 (ca. 30, 000 daltons) has been split into smaller segments, two of which VP3a and VP3b have molecular weights of about 15, 000 daltons (Bachrach, et al., 1975).Highly purified and concentrated type A12, strain 119 FMDV (5 mg/ml) was prepared as previously described (Bachrach, et al., 1964) and stored at 4°C in 0. 2 M KC1-0. 5 M potassium phosphate buffer at pH 7. 5. For electron microscopy, 1. 0 ml samples of purified virus and trypsin-treated virus were dialyzed at 4°C against 0. 2 M NH4OAC at pH 7. 3, deposited onto carbonized formvar-coated copper screens and stained with phosphotungstic acid, pH 7. 3.

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