Structural proteins of equine arteritis virus

Hyllseth, B.

doi:10.1007/bf01242536

Cited by 33 publications

(32 citation statements)

References 16 publications

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“…After detergent treatment of virus particles, only the smallest virion protein cosedimented with the viral genome in a sucrose gradient (24,58). This indicates that the 14-kDa virion protein corresponds to the nucleocapsid protein and implies that the other structural proteins are either envelope or matrix proteins.…”

Section: Discussionmentioning

confidence: 99%

“…The virions consist of an isometric nucleocapsid of about 35 nm which is surrounded by an envelope with ringlike surface substructures (20,25). The nucleocapsid is composed of an infectious, polyadenylated, single-stranded genomic RNA with a size of 12.7 kb (7) and a 12-to 14-kDa phosphorylated core protein (24,58). The envelope contains a 14-to 16- glycoproteins (24,51,58); the latter have not been unambiguously defined.…”

mentioning

confidence: 99%

“…The nucleocapsid is composed of an infectious, polyadenylated, single-stranded genomic RNA with a size of 12.7 kb (7) and a 12-to 14-kDa phosphorylated core protein (24,58). The envelope contains a 14-to 16- glycoproteins (24,51,58); the latter have not been unambiguously defined. In some studies, a glycosylated 21-kDa protein has been detected, while in others, a heterogeneously migrating set of glycoproteins in the size range of 28 to 40 kDa has been reported.…”

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confidence: 99%

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The structural proteins of equine arteritis virus

1976

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We have recently shown that the genome of equine arteritis virus (EAV) contains seven open reading frames (ORFs). We now present data on the structural proteins of EAV and the assignment of their respective genes.Virions are composed of a 14-kDa nucleocapsid protein (N) and three membrane proteins designated M, Gs, and GL. M is an unglycosylated protein of 16 kDa, and GS and GL are N-glycosylated proteins of 25 and 30 to 42 kDa, respectively. The broad size distribution of GL results from heterogeneous N-acetyllactosamine addition since it is susceptible to digestion by endo-o-galactosidase. Using monospecific antisera as well as an antivirion serum, and by expression of individual ORFs, the genes for the structural proteins were identified: ORF 7 codes for N, ORF 6 for M, ORF 5 for GL, and ORF 2 for GS. With the exception of GS, the proteins are about equally abundant in EAV virions, being present at a molar ratio of 3 (N):2 (M):3 (GL). The GS protein, which is expressed at a level similar to that of M in infected cells, is strikingly underrepresented in virus particles (1 to 2%). Our data justify a distinct taxonomic position for EAV, together with lactate dehydrogenase-elevating virus and simian hemorrhagic fever virus; although coronavirus-and toroviruslike in features of transcription and translation, the virion architecture of EAV is fundamentally different.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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confidence: 99%

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The structural proteins of equine arteritis virus

1976

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“…13,16 Conflicting and often contradictory descriptions of the proteins of EAV have been provided in previous studies; a considerable number of apparently different virus-specific proteins of molecular masses of 10.5-72 kD have been identified in EAV-infected cells. 12,13,[28][29][30]52,53,56 The problem of accurately determining the specific identity of individual EAV proteins in the immunoblotting assay is magnified by the similar molecular masses of the G L and G S proteins and of the N and M proteins. The variable glycosylation of the G L and G S proteins 13 and dimerization of the envelope proteins further confuses identification of the structural proteins of EAV.…”

Section: Discussionmentioning

confidence: 99%

“…27,28 The EAV particle consists of 4 structural proteins, including a phosphorylated nucleocapsid protein (N) and 3 membrane proteins designated M, G S , and G L . 13 The M protein is an unglycosylated protein of 16 kD, and G S and G L are N-glycosylated proteins of 25 and 30-42 kD, respectively.…”

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Serologic Response of Horses to the Structural Proteins of Equine Arteritis Virus

et al. 1998

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Abstract. Equine arteritis virus (EAV) is the causative agent of equine viral arteritis, an apparently emerging disease of equids. In this study, the antibody response of horses to the structural proteins of EAV was evaluated using gradient-purified EAV virions and baculovirus-expressed recombinant EAV structural proteins (G L , G S , M, N) as antigens in a Western immunoblotting assay. Thirty-three sera from horses that previously had been naturally or experimentally infected with EAV were evaluated, including samples from mares, geldings, and both persistently and nonpersistently infected stallions. Sera also were evaluated from 4 horses that had been vaccinated with the commercial modified live EAV vaccine. The data suggest that the serologic response of individual horses to EAV may vary with the infecting virus strain and duration of infection. The M protein was most consistently recognized by the various serum samples, whereas the response to the N and G L proteins was variable and the G S protein was bound by only 1 serum sample. The immunoblotting assay definitively established the protein specificity of the humoral response of horses to EAV; however, it clearly is less sensitive than the standard serum neutralization (SN) test-2 of the 37 sera that were seropositive by the SN test failed to react in the immunoblot assay with any EAV structural protein. Furthermore, the G L protein expresses the known neutralization determinants of EAV, yet only 22 of the 37 sera that had SN antibodies bound the G L protein in the immunoblotting assay. Information from this study will assist ongoing efforts to develop improved methods for the serologic diagnosis of EAV infection of horses.Equine arteritis virus (EAV) is the causative agent of equine viral arteritis (EVA), a disease of horses that may manifest as interstitial pneumonia in very young foals, influenza-like illness of adult horses, and abortion of pregnant mares. 6,10,18,19,22,31,43,45,51 Persistently infected stallions that shed virus in their semen are a critical natural reservoir of EAV because venereal infection of mares frequently occurs after mating with such stallions. 26,34,40,[44][45][46][47]50 Horizontal spread of the virus occurs via aerosol exposure of susceptible horses to acutely infected animals. 38,44,45 EAV infection is especially prevalent in Standardbred horses, but since the mid-1980s there has been a disturbing increase in the incidence of EVA in a variety of horse breeds. 5,20,24,25,39,44,45,48,49 EAV is an enveloped, positive-stranded RNA virus 27,36,37,41 that recently was taxonomically placed in the genus Arterivirus in the order Nidovirales, along with porcine reproductive and respiratory syndrome virus, lactate dehydrogenase-elevating virus, and simian hemorrhagic fever virus. 7 The EAV virion has a diameter of approximately 55 nm and consists of a

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Genetic Manipulation of Equine Arteritis Virus Using Full-Length cDNA Clones: Separation of Overlapping Genes and Expression of a Foreign Epitope

et al. 2000

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Equine arteritis virus (EAV) is an enveloped, positive-stranded RNA virus belonging to the family Arteriviridae of the order Nidovirales. The unsegmented, infectious genome of EAV is 12,704 nt in length [exclusive of the poly(A) tail] and contains eight overlapping genes that are expressed from a 3'-coterminal nested set of seven leader-containing mRNAs. To investigate the importance of the overlapping gene arrangement in the viral life-cycle and to facilitate the genetic manipulation of the viral genome, a series of mutant full-length cDNA clones was constructed in which either EAV open reading frames (ORFs) 4 and 5 or ORFs 5 and 6 or ORFs 4, 5, and 6 were separated by newly introduced AflII restriction endonuclease cleavage sites. RNA transcribed from each of these plasmids was infectious, demonstrating that the overlapping gene organization is not essential for EAV viability. Moreover, the recombinant viruses replicated with almost the same efficiency, i.e., reached nearly the same infectious titers as the wildtype virus, and stably maintained the mutations that were introduced. The AflII site engineered between ORFs 5 and 6 was subsequently used to generate a virus in which the ectodomain of the ORF 6-encoded M protein was extended with nine amino acids derived from the extreme N-terminus of the homologous protein of mouse hepatitis virus (MHV; family Coronaviridae, order Nidovirales). This nonapeptide contains a functional O-glycosylation signal as well as an epitope recognized by an MHV-specific monoclonal antibody, both of which were expressed by the recombinant virus. Although the hybrid virus had a clear growth disadvantage in comparison to the parental virus, three serial passages did not result in the loss of the foreign genetic material.

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Structural proteins of equine arteritis virus

Cited by 33 publications

References 16 publications

The structural proteins of equine arteritis virus

The structural proteins of equine arteritis virus

Serologic Response of Horses to the Structural Proteins of Equine Arteritis Virus

Genetic Manipulation of Equine Arteritis Virus Using Full-Length cDNA Clones: Separation of Overlapping Genes and Expression of a Foreign Epitope

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