Inhibition of cell-free foot-and-mouth disease virus-ribonucleic acid synthesis by antibody

Polatnick, Jerome; Arlinghaus, Ralph B.; Graves, J. H.; Cowan, K. M.

doi:10.1016/0042-6822(67)90189-4

Cited by 40 publications

(8 citation statements)

References 8 publications

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“…Therefore it is possible that the amino terminus of 3D is responsible for the processing of sites we have attributed to 3C. This is highly unlikely, because 3D is associated with an RNA-dependent RNA polymerase activity (14,40), whereas 3C has been shown to be a protease (29).…”

Section: Discussionmentioning

confidence: 98%

Proteolytic processing of foot-and-mouth disease virus polyproteins expressed in a cell-free system from clone-derived transcripts

Vakharia¹,

Devaney²,

Moore³

et al. 1987

J Virol

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All picornaviral genes are expressed as a single, large polyprotein, which is proteolytically processed into the mature proteins. Cell-free translation of foot-and-mouth disease virus (FMDV) RNA in a rabbit reticulocyte system produces functional proteins, including viral protease 3C, which plays a major role in processing the precursor proteins. To study the function of the two putative proteases 3C and leader (L) in processing, we constructed several cDNA plasmids encoding various regions of the FMDV type A12 genome. These plasmids, containing FMDV cDNA segments under the control of the T7 promoter, were transcribed in vitro by using T7 RNA polymerase and then translated in rabbit reticulocyte lysates. The expressed FMDV gene products were identified by immunoprecipitation with specific antisera and analyzed by gel electrophoresis. The results demonstrate the following: (i) the leader protein, L, is processed from the structural protein precursor, P1, in the absence of any P2 or P3 region proteins; (ii) protein 2A remains associated with the structural protein precursor, P1, rather than the precursor, P2; (iii) the processing of the P1-2A/P2 junction is not catalyzed by 3C or L; (iv) the proteolytic processing of polyproteins from the structural P1 region (except VP4/VP2) and the nonstructural P2 and P3 region is catalyzed by 3C.

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Section: Discussionmentioning

confidence: 98%

Proteolytic processing of foot-and-mouth disease virus polyproteins expressed in a cell-free system from clone-derived transcripts

Vakharia¹,

Devaney²,

Moore³

et al. 1987

J Virol

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“…pro was identified as a viral protease (252) and is involved in processing the viral polyprotein, while 3D pol is the viral RNAdependent RNA polymerase (110,275,335,(368)(369)(370)389). The roles that each of these proteins play in viral replication are discussed in Infectious Cycle below.…”

Section: Description Of the Agent Genome Organizationmentioning

confidence: 99%

Foot-and-Mouth Disease

2004

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Foot-and-mouth disease (FMD) is a highly contagious disease of cloven-hoofed animals. The disease was initially described in the 16th century and was the first animal pathogen identified as a virus. Recent FMD outbreaks in developed countries and their significant economic impact have increased the concern of governments worldwide. This review describes the reemergence of FMD in developed countries that had been disease free for many years and the effect that this has had on disease control strategies. The etiologic agent, FMD virus (FMDV), a member of the Picornaviridae family, is examined in detail at the genetic, structural, and biochemical levels and in terms of its antigenic diversity. The virus replication cycle, including virus-receptor interactions as well as unique aspects of virus translation and shutoff of host macromolecular synthesis, is discussed. This information has been the basis for the development of improved protocols to rapidly identify disease outbreaks, to differentiate vaccinated from infected animals, and to begin to identify and test novel vaccine candidates. Furthermore, this knowledge, coupled with the ability to manipulate FMDV genomes at the molecular level, has provided the framework for examination of disease pathogenesis and the development of a more complete understanding of the virus and host factors involved

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“…On the basis of these experiments Cowan & Graves (I966) suggested that the VIA antigen was a non-structural protein. Polatnick et al (1967) showed that VIA antibody inhibited the viral RNA polymerase in vitro and concluded that the antigen was an inactive form of the enzyme since they could not detect any polymerase activity in the VIA antigen preparations. The VIA antigens from all seven serotypes of the virus were indistinguishable in complement fixation and immunodiffusion tests (Cowan & Graves,I966).…”

Section: Introductionmentioning

confidence: 99%

Characterization of the Minor Polypeptides in the Foot-and-Mouth Disease Particle

Sangar

Rowlands

Cavanagh

et al. 1976

Journal of General Virology

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SUMMARYIn addition to the four major polypeptides VPI to VP4, foot-and-mouth disease virus particles contain two minor polypeptides, tool. wt. 4ox lO 3 (P4o) and 52 × Io a (P52). Extensive purification procedures failed to remove these minor polypeptides from the virus particles. Polypeptide P4o co-electrophoresed in SDSpolyacrylamide gels with VPo, the probable precursor of VP2 and VP 4 and was inaccessible to iodination in situ. The second minor polypeptide, P52, co-electrophoresed with the virus infection associated (VIA) antigen found in large amounts in harvests of the virus grown in BHK 2I cells. Polypeptide P52 was shown to be located near the surface of the virus particle by iodination experiments and by its removal on incubating the particles with trypsin or chymotrypsin. Pactamycin mapping showed that this polypeptide was not a precursor of the structural polypeptides. About one copy of P52 and 4 copies of P4o were found in the virus particles sedimenting at I46 S. However a larger number of copies was found in those virus particles sedimenting faster than the I46 S peak.

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Inhibition of cell-free foot-and-mouth disease virus-ribonucleic acid synthesis by antibody

Cited by 40 publications

References 8 publications

Proteolytic processing of foot-and-mouth disease virus polyproteins expressed in a cell-free system from clone-derived transcripts

Proteolytic processing of foot-and-mouth disease virus polyproteins expressed in a cell-free system from clone-derived transcripts

Foot-and-Mouth Disease

Characterization of the Minor Polypeptides in the Foot-and-Mouth Disease Particle

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