'Blue ear' disease of pigs

Paton, D.J.; Brown, IH; Edwards, Susanna; Wensvoort, G.

doi:10.1136/vr.128.26.617

Cited by 73 publications

(48 citation statements)

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“…PRRS has also recently been confirmed to have been present in Japan since 1989 (Shimizu et al, 1994), where it is known as Heko-Heko. The disease was first confirmed in Britain in the spring of 1991 (Paton et al, 1991) at about the same time as the specific viral aetiology of the disease was established . In the next 18 months the virus, now shown to be an arterivirus (Meulenberg et al, 1993), spread to several regions in Britain where it caused a very varied spectrum of disease .…”

Section: Introductionmentioning

confidence: 93%

Production, characterization and reactivity of monoclonal antibodies to porcine reproductive and respiratory syndrome virus

Drew

Meulenberg²,

Sands

et al. 1995

Journal of General Virology

101

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Section: Introductionmentioning

confidence: 93%

Production, characterization and reactivity of monoclonal antibodies to porcine reproductive and respiratory syndrome virus

Drew

Meulenberg²,

Sands

et al. 1995

Journal of General Virology

101

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“…Although sequence similarities between North American and European isolates of PRRSV show they arose from a common ancestor, it is apparent that these groups of isolates diverged before the recent appearance of disease in the last decade (Hill, 1990;Paton et al, 1991). However, within the midwestern US it is of interest to determine whether the outbreak of disease is consistent with the appearance of a single viral type which then radiated, or whether numerous genetically distinct types were present, one or more of which were responsible for the new disease.…”

Section: How Old Is the Prrs Virus ?mentioning

confidence: 99%

“…A new viral disease of pigs was detected in North America in 1987 (Hill, 1990) and in Europe in 1990 (Paton et al, 1991). The disease, now known as porcine reproductive and respiratory syndrome (PRRS), is characterized by late-term abortions and stillbirths in sows and respiratory difficulties in nursery pigs (Pol et at., 1991;Collins et al, 1992).…”

Section: Introductionmentioning

confidence: 99%

Genetic variation in porcine reproductive and respiratory syndrome virus isolates in the midwestern United States

Hudson

Elam

Pawlovich

et al. 1996

Journal of General Virology

224

162

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The nucleotide sequence of a 3266 bp region encompassing open reading frames (ORFs) 2 through 7 of the porcine reproductive and respiratory syndrome virus (PRRSV) was determined for 10 isolates recovered from the midwestern United States. Pairwise comparisons showed that genetic distances between isolates ranged from 2.5 % to 7.9 % (mean 5.8 % + 0.2 %) whereas the Lelystad strain from Europe was, on average, 34-8 % divergent from US clones. Thus, US and European PRRSV isolates represent genetically distinct clusters of the same virus. ORF 5, which encodes the envelope glycoprotein, was the most polymorphic [total nucleotide diversity (re) = 0-097 __+ 0"007] and ORF 6, encoding the viral M protein, was the most conserved (n = 0"038 ___ 0"003). The substantial differences in nucleotide diversity among ORFs suggests that the virus is evolving by processes other than simple accumulation of random neutral mutations. In support of this hypothesis, statistical analyses of the nucleotide sequence provided strong evidence for intragenic recombination or gene conversion in ORFs 2, 3, 4, 5 and 7, but not in ORF 6.An excess of synonymous (silent) substitutions was observed in all six ORFs, indicating an evolutionary pressure to conserve amino acid sequences. Taken together, the data indicate that despite intragenic recombination among extant PRRSV isolates, purifying selection has acted to maintain the primary structure of individual ORFs.

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“…This economically devastating, pandemic disease causes reproductive failure in breeding stock and respiratory tract illness in young pigs. Initially referred to as a "mystery swine disease" and a "mystery reproductive syndrome," it was first reported in 1987 in North America (VR-2332 strain) (1) and central Europe (Lelystad Virus/LV strain) (26). Although the European and North American PRRSV strains cause similar clinical symptoms, they represent two distinct major viral genotypes, with their genomes diverging by approximately 40% (30).…”

mentioning

confidence: 99%

Crystal Structure of Porcine Reproductive and Respiratory Syndrome Virus Leader Protease Nsp1α

Sun

Guo

et al. 2009

J Virol

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Porcine reproductive and respiratory syndrome (PRRS) virus (PRRSV), a positive-strand RNA virus that belongs to the Arteriviridae family of Nidovirales, has been identified as the causative agent of PRRS. Nsp1␣ is the amino (N)-terminal protein in a polyprotein encoded by the PRRSV genome and is reported to be crucial for subgenomic mRNA synthesis, presumably by serving as a transcription factor. Before functioning in transcription, nsp1␣ proteolytically releases itself from nsp1␤. However, the structural basis for the selfreleasing and biological functions of nsp1␣ remains elusive. Here we report the crystal structure of nsp1␣ of PRRSV (strain XH-GD) in its naturally self-processed form. Nsp1␣ contains a ZF domain (which may be required for its biological function), a papain-like cysteine protease (PCP) domain with a zinc ion unexpectedly bound at the active site (which is essential for proteolytic self-release of nsp1␣), and a carboxyl-terminal extension (which occupies the substrate binding site of the PCP domain). Furthermore, we determined the exact location of the nsp1␣ self-processing site at Cys-Ala-Met1802Ala-Asp-Val by use of crystallographic data and N-terminal amino acid sequencing. The crystal structure also suggested an in cis self-processing mechanism for nsp1␣. Furthermore, nsp1␣ appears to have a dimeric architecture both in solution and as a crystal, with a hydrophilic groove on the molecular surface that may be related to nsp1␣'s biological function. Compared with existing structure and function data, our results suggest that PRRSV nsp1␣ functions differently from other reported viral leader proteases, such as that of foot-and-mouth disease.

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'Blue ear' disease of pigs

Cited by 73 publications

References 0 publications

Production, characterization and reactivity of monoclonal antibodies to porcine reproductive and respiratory syndrome virus

Production, characterization and reactivity of monoclonal antibodies to porcine reproductive and respiratory syndrome virus

Genetic variation in porcine reproductive and respiratory syndrome virus isolates in the midwestern United States

Crystal Structure of Porcine Reproductive and Respiratory Syndrome Virus Leader Protease Nsp1α

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