Distinctive features of foot-and-mouth disease virus, a member of the picornavirus family; aspects of virus protein synthesis, protein processing and structure

Belsham, Graham J.

doi:10.1016/0079-6107(93)90016-d

Cited by 299 publications

(180 citation statements)

References 96 publications

(97 reference statements)

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“…The genome of FMDV is a positive-sense RNA of about 8 . 5 kb which encodes a polyprotein that is processed to the four structural proteins (VP1-VP4) of the virus capsid (only VP1-VP3 are surface exposed) plus several nonstructural proteins required for virus replication and protein processing [2]. FMDV occurs in seven immunologically distinct serotypes namely O, A, C, Southern African Territories (SAT) 1-3, and Asia 1.…”

Section: Introductionmentioning

confidence: 99%

Low diversity of foot-and-mouth disease serotype C virus in Kenya: evidence for probable vaccine strain re-introductions in the field

Sangula

Siegismund²,

Belsham

et al. 2010

Epidemiol. Infect.

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SUMMARYMost viruses are maintained by complex processes of evolution that enable them to survive but also complicate efforts to achieve their control. In this paper, we study patterns of evolution in foot-and-mouth disease (FMD) serotype C virus isolates from Kenya, one of the few places in the world where serotype C has been endemic and is suspected to remain. The nucleotide sequences encoding the capsid protein VP1 from eight isolates collected between 1967 and 2004 were analysed for patterns of sequence divergence and evolution. Very low nucleotide diversity (π=0·0025) and remarkably little change (only five segregating sites and three amino-acid changes) were observed in these isolates collected over a period of almost 40 years. We interpret these results as being suggestive of re-introductions of the vaccine strain into the field. The implications of these results for the maintenance of serotype C FMD virus and the use of vaccination as a control measure in Kenya are discussed.

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Section: Introductionmentioning

confidence: 99%

Low diversity of foot-and-mouth disease serotype C virus in Kenya: evidence for probable vaccine strain re-introductions in the field

Sangula

Siegismund²,

Belsham

et al. 2010

Epidemiol. Infect.

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“…The 2A protease cleaves itself at its C terminus to release P1-2A from P2. Processing of P1-2A is effected by the 3C protease to produce the capsid proteins lAB (VP0), 1C (VP3) and 1D (VP1) (for review see Belsham, 1993). In the virion, cleavage of lAB occurs to produce IA (VP4) and 1B (VP2).…”

Section: Introductionmentioning

confidence: 99%

Assembly of foot-and-mouth disease virus empty capsids synthesized by a vaccinia virus expression system

Abrams

King

Belsham

1995

Journal of General Virology

102

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cDNA cassettes encoding the foot-and-mouth disease virus (FMDV) structural protein precursor (P1-2A) together with the 3C protease, which cleaves this molecule to lAB, 1C and 1D, were constructed. These cassettes were introduced into vaccinia virus (VV) transfer vectors. Attempts to isolate recombinant Ws constitutively expressing these cassettes were unsuccessful. However, when the P1-2A-3C cassette was placed under the control of the bacteriophage T7 promoter, stable VV/FMDV recombinants were isolated. Co-infection with recombinant VV vTF7-3 (which expresses T7 RNA polymerase) led to the production of correctly processed FMDV capsid proteins. Analysis by sucrose gradient centrifugation showed that material which co-sedimented with natural empty capsid particles (70S) was formed. Electron microscopy revealed empty capsid-like particles with diameters of about 30 nm. Studies using monoclonal antibodies specific for conformational epitopes indicated that the antigenicity of the synthetic particles was similar to whole virions and natural empty capsid particles. Surprisingly, merely the modification of a single amino acid residue within the myristoylation consensus sequence at the N terminus of P 1-2A allowed the isolation of a recombinant VV which constitutively expressed the correctly processed proteins. However, the capsid proteins expressed from this mutant cassette failed to assemble into 70S empty particles.

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“…There are seven serotypes of FMDV that all belong to the Aphthovirus genus of the family Picornaviridae (2).…”

mentioning

confidence: 99%

VP1 of Foot-and-Mouth Disease Virus Induces Apoptosis via the Akt Signaling Pathway

Peng

Liang

2004

Journal of Biological Chemistry

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Distinctive features of foot-and-mouth disease virus, a member of the picornavirus family; aspects of virus protein synthesis, protein processing and structure

Cited by 299 publications

References 96 publications

Low diversity of foot-and-mouth disease serotype C virus in Kenya: evidence for probable vaccine strain re-introductions in the field

Low diversity of foot-and-mouth disease serotype C virus in Kenya: evidence for probable vaccine strain re-introductions in the field

Assembly of foot-and-mouth disease virus empty capsids synthesized by a vaccinia virus expression system

VP1 of Foot-and-Mouth Disease Virus Induces Apoptosis via the Akt Signaling Pathway

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