Foot-and-mouth disease virus-induced ribonucleic acid polymerase in baby hamster kidney cells

Polatnick, Jerome; Arlinghaus, Ralph B.

doi:10.1016/0042-6822(67)90188-2

Cited by 55 publications

(36 citation statements)

References 10 publications

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“…In 1966 Cowan and Graves (4) reported the presence of a group-specific protein (VIA antigen of 56 kDa) in FMDVinfected cells, which was later identified as the virus RNA polymerase (5,20,21). Rowlands et al (9) demonstrated that antiserum raised in guinea pigs against purified inactivated virus particles also reacted with the VIA antigen and argued that the failure of Cowan and Graves (4) to detect the reaction with antiserum from vaccinated animals could have been because insufficient virus particles had been inoculated.…”

Section: Discussionmentioning

confidence: 99%

“…Polymerase activity was determined in a poly(A) polymerase assay as described by Sankar and Porter (16). Briefly, a 50-,ul reaction mixture containing [1][2][3][4][5][6][7][8] ,ug of recombinant polymerase, 2.5 ,g of poly(A), 1 ,g of oligo (U), 10 ,uM UTP, 5 ,uCi of [3H]UTP (1 Ci = 37 GBq), 5 mM dithiothreitol, 3.5 mM magnesium acetate, and 6 ,LM zinc chloride in 50 mM Hepes (pH 8) after 60 min at 30°C was precipitated with 10% (wt/vol) trichloroacetic acid with 100 ug of carrier tRNA. The precipitates were divided into two aliquots and collected on nitrocellulose filters (Millipore).…”

Section: Methodsmentioning

confidence: 99%

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Foot-and-mouth disease virus particles contain replicase protein 3D.

Newman

Piatti

Gorman

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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An antibody against the Escherichia coliexpressed RNA polymerase of foot-and-mouth disease virus (FMDV) reacts with the virus in ELISA and radioimmunoprecipitation experiments and with a protein of the disrupted virus particle in an immunoblot analysis. Treatment of the virus with trypsin, which cleaves capsid protein VP1 and a 56-kDa polypeptide present in trace amount in the particles, reduces the level of the reaction in ELISA and radioimmunoprecipitation and eliminates the immunoblot reaction. Electron microscopy showed that only --20% of the virus particles reacted with the anti-polymerase antibody, whereas most reacted with an antibody against the immunodominant G-H loop of the virus. In the presence of ammonium ions, the expressed polymerase degrades the RNA of the virus into molecules sedimenting at "'12 S, indicating that it can act as a hydrolytic as well as a polymeriznng enzyme. Moreover, the RNA in trypsin-treated virus particles is degraded when incubated at 3rC, suggesting that the cleaved 56-kDa protein still possesses hydrolytic activity. In addition, the anti-polymerase antibody, which inhibits the polymerase activity of the E. col-expressed protein, also partially inhibits the hydrolytic activity of the previously described endonuclease of the virus particle, suggesting that this enzyme is identical with the polymerase or forms part of it.Although it is generally accepted that picornaviruses consist of one molecule of positive-sense single-stranded RNA of -2600 kDa, the four capsid proteins VP1-VP4 (each present in 60 copies), and one or two copies of VP0 (the precursor of VP4 and VP2), traces of other proteins of 40 kDa and 56 kDa have been found consistently in highly purified particles of foot-and-mouth disease virus (FMDV) (1, 2). J.F.E.N. (unpublished observation) has also found traces of proteins of similar size in poliovirus particles. The 56-kDa protein in FMDV is phosphorylated (3) and, with one of the two proteins of 40 kDa, is cleaved by treating the particles with trypsin (2). With the exception of VPO (40 kDa), to our knowledge, the identity of these minor polypeptides has not been established with certainty. Biochemical mapping indicated that in addition to VP0 a second protein of 40 kDa was present. This protein was encoded downstream of the capsid proteins (2), and the 56-kDa protein was considered to be the virus-infection-associated (VIA) antigen (the viral RNA polymerase; refs. 4 and 5) on the basis of its molecular mass and its reaction with serum from convalescent and vaccinated animals.Because of their failure to detect antibody to the VIA antigen in the sera of vaccinated animals, in contrast to its presence in convalescent sera, Cowan and Graves (4) concluded that its presence was associated with infection. However, recent work has demonstrated (6-8) the presence ofThe publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate t...

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Foot-and-mouth disease virus particles contain replicase protein 3D.

Newman

Piatti

Gorman

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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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%

“…The major reason that antibodies against an NS protein are present in sera from vaccinated animals is that FMD vaccines are not purified and, depending upon the manufacturer, contain various amounts of contaminating NS proteins (277). Nevertheless VIAA, which was subsequently identified as the viral RNA polymerase (3D pol ) (335,369), is currently used in an agar-gel immunodiffusion test to differentiate infected from vaccinated animals.…”

Section: Disease Controlmentioning

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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“…e) Not tested. basis of its molecular mass and its reaction with sera from convalescent animals [5,14]. FMDV particles have been shown to react with antibody against recombinant 3D, which demonstrates that 3D is a component of FMDV particles [13].…”

mentioning

confidence: 99%

Differentiation of Foot-and-Mouth Disease Virus-Infected Pigs from Vaccinated Pigs using a Western Blotting Assay Based on Baculovirus-Expressed Nonstructural Proteins 2C and 3D

Fukai

Morioka

Ohashi

et al. 2008

The Journal of Veterinary Medical Science

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ABSTRACT. Baculovirus-expressed foot-and-mouth disease virus (FMDV) nonstructural proteins 2C and 3D were used as the antigens in a western blotting assay. This assay allowed for differentiation of FMDV-infected pigs from vaccinated pigs. Serial studies were performed using sera collected from experimentally infected and vaccinated pigs. Positive reactions were found in the sera derived from the experimentally infected pigs. There was, however, no positive reaction in the vaccinated pigs. These results suggest that this western blotting assay is a useful method for differentiation of infected pigs from vaccinated pigs. KEY WORDS: baculovirus, foot-and-mouth disease virus, nonstructural protein, swine, western blotting.

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Foot-and-mouth disease virus-induced ribonucleic acid polymerase in baby hamster kidney cells

Cited by 55 publications

References 10 publications

Foot-and-mouth disease virus particles contain replicase protein 3D.

Foot-and-mouth disease virus particles contain replicase protein 3D.

Foot-and-Mouth Disease

Differentiation of Foot-and-Mouth Disease Virus-Infected Pigs from Vaccinated Pigs using a Western Blotting Assay Based on Baculovirus-Expressed Nonstructural Proteins 2C and 3D

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