Lactate Dehydrogenase-Elevating Virus, Equine Arteritis Virus, and Simian Hemorrhagic Fever Virus: A New Group of Positive-Strand RNA Viruses

Plagemann, Peter G.W.; Moennig, V.

doi:10.1016/s0065-3527(08)60036-6

Cited by 300 publications

(306 citation statements)

References 238 publications

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“…These intracellular budding viruses are very similar both structurally and with respect to their replication (Plagemann & Moennig, 1992;Conzelmann et al, 1993). Interestingly, comparative analysis of the predicted ORF 5 products of these viruses revealed a number of conserved features indicating that despite the absence of significant sequence similarities these proteins are the structural homologues of the EAV G L protein.…”

Section: Discussionmentioning

confidence: 99%

“…The Arteriviridae is currently comprised of EAV, lactate dehydrogenase-elevating virus (LDV), simian haemorrhagic fever virus and porcine respiratory and reproductive syndrome virus (PRRSV) (Plagemann & Moennig, 1992;Cavanagh et al, 1994). These intracellular budding viruses are very similar both structurally and with respect to their replication (Plagemann & Moennig, 1992;Conzelmann et al, 1993).…”

Section: Discussionmentioning

confidence: 99%

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Equine arteritis virus-neutralizing antibody in the horse is induced by a determinant on the large envelope glycoprotein GL

Chirnside

Vries

Mumford

et al. 1995

Journal of General Virology

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Complementary DNAs encoding ORFs 2 to 7 of equine arteritis virus (EAV) have been cloned into the expression vector pGEX to produce glutathione-S-transferase fusion proteins. Recombinant proteins were affinity purified and screened in ELISA with equine sera to identify immunoreactive polypeptides. The large envelope glycoprotein (GL) was identified as the most reactive to EAV-positive equine sera and an immunodominant epitope was mapped between amino acids 55 and 98 by subcloning and expression. A fusion protein covering this region and a GL-Specific synthetic peptide (residues 75 through 97) induced EAV-nentralizing antibody in vaccinated horses. The defined antigenic region of G L is likely to be exposed on the surface of the native EAV virion and consequently may be useful in the development of diagnostic tests and vaccines.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Equine arteritis virus-neutralizing antibody in the horse is induced by a determinant on the large envelope glycoprotein GL

Chirnside

Vries

Mumford

et al. 1995

Journal of General Virology

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“…The nidovirus order comprises a group of evolutionarily related enveloped, positive-stranded RNA virus families (arteri-, corona-, and roniviruses) [7,10,12,33]. PRRSV infection is characterized by reproductive failure in sows and by respiratory § These authors contributed equally to this work.…”

Section: Introductionmentioning

confidence: 99%

Involvement of proteases in porcine reproductive and respiratory syndrome virus uncoating upon internalization in primary macrophages

2008

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-Porcine reproductive and respiratory syndrome virus (PRRSV) replicates in differentiated macrophages. In macrophages, heparan sulphate glycosaminoglycans mediate the initial PRRSV attachment and the receptor sialoadhesin mediates both PRRSV attachment and internalization into endosomes. Upon a pH drop, PRRSV is uncoated and its genome is released from the endosomes into the cytoplasm, which allows virus replication. However, expression of heparan sulphate and sialoadhesin in non-susceptible cells only allows virus internalization, but no virus uncoating and infection, indicating that other factors are involved. In the present study, it is shown that treatment of macrophages with serum (mainly the alpha-globulin fraction) inhibited PRRSV infection without affecting attachment and internalization. Because alpha-globulins contain several protease inhibitors, macrophages were treated with different protease inhibitors to investigate the involvement of proteases in PRRSV uncoating. Treatment of macrophages with broadly active inhibitors of serine or aspartic proteases, but not cysteine-or metallo-proteases, inhibited PRRSV uncoating and infection. Further investigation using specific inhibitors indicated that the aspartic protease cathepsin E is involved during PRRSV uncoating, but did not allow identification of the serine protease involved. The involvement of cathepsin E during PRRSV uncoating was confirmed by partial co-localization of internalized PRRSV with cathepsin E. Furthermore, cathepsin E expression increased with macrophage cultivation, which was positively correlated with an increased susceptibility to PRRSV infection. Together, these data show that, in macrophages, both the aspartic protease cathepsin E and an unidentified trypsin-like serine protease are involved in uncoating of internalized PRRSV and subsequent infection. porcine arterivirus / macrophage / virus entry / protease / receptor

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“…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…”

mentioning

confidence: 99%

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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Lactate Dehydrogenase-Elevating Virus, Equine Arteritis Virus, and Simian Hemorrhagic Fever Virus: A New Group of Positive-Strand RNA Viruses

Cited by 300 publications

References 238 publications

Equine arteritis virus-neutralizing antibody in the horse is induced by a determinant on the large envelope glycoprotein GL

Equine arteritis virus-neutralizing antibody in the horse is induced by a determinant on the large envelope glycoprotein GL

Involvement of proteases in porcine reproductive and respiratory syndrome virus uncoating upon internalization in primary macrophages

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

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