Acute Encephalitis and Hydrocephalus in Dogs Caused by Canine Parainfluenza Virus

Baumgärtner, Wolfgang; Krakowka, Steven; Koestner, A.; Evermann, James F.

doi:10.1177/030098588201900111

Cited by 44 publications

(26 citation statements)

References 20 publications

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“…In dogs, SV5 commonly causes minor respiratory tract infections, although the virus has also been recovered from the cerebrospinal fluid of a dog v~ith temporary posterior paralysis (Baumgartner et al, 1981). This particular isolate has subsequently been shown to cause experimentally induced encephalitis when inoculated into gnotobiotic dogs (Baumgartner et at., 1982). Because SV5 commonly infects dogs the virus is usually referred to in veterinary circles as canine parainfluenza virus.…”

Section: Introductionmentioning

confidence: 99%

Isolation and Characterization of Monoclonal Antibodies to Simian Virus 5 and Their Use in Revealing Antigenic Differences between Human, Canine and Simian Isolates

Randall

Young

Goswami

et al. 1987

Journal of General Virology

157

137

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SUMMARYHybridomas secreting monoclonal antibodies to simian virus 5 (SV5) were obtained following immunization of mice with purified preparations of a human isolate (LN) of SV5. Immune precipitation studies showed that these monoclonal antibodies had specificities for the haemagglutinin-neuraminidase (HN), fusion (F), nucleo-, matrix and phospho-(P) proteins of SV5. By use of a radioimmune competition assay the monoclonal antibodies to the HN protein were assigned to four groups, members of which recognized different antigenic sites on the protein. All the anti-HN antibodies and the anti-F antibody neutralized virus infectivity. The 54 monoclonal antibodies obtained were used to determine whether there were antigenic differences between five human, two canine and one simian isolate of SV5. Although most of the monoclonal antibodies reacted with all isolates, a few did reveal antigenic differences in the HN, F and P proteins. Furthermore, analysis by SDS-PAGE showed that while the electrophoretic mobilities of most of the virus polypeptides of these isolates were similar some differences could be detected. In particular the P protein showed the most marked mobility differences between the human, canine and simian isolates. Slight differences in the mobility of the F1 glycoprotein could also be visualized.

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Section: Introductionmentioning

confidence: 99%

Isolation and Characterization of Monoclonal Antibodies to Simian Virus 5 and Their Use in Revealing Antigenic Differences between Human, Canine and Simian Isolates

Randall

Young

Goswami

et al. 1987

Journal of General Virology

157

137

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“…During the course of studying the CPIϩ virus, a derivative of CPIϩ, termed CPIϪ, was isolated from a dog that was experimentally infected with the CPIϩ virus (2). It was found that there are differences among the V/P genes of CPIϩ, CPIϪ, and the commonly used lab strain W3A, in addition to differences in other viral genes (4,5,35).…”

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A Single Amino Acid Residue Change in the P Protein of Parainfluenza Virus 5 Elevates Viral Gene Expression

Timani

Sun

et al. 2008

J Virol

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Parainfluenza virus 5 (PIV5) is a prototypical paramyxovirus. The V/P gene of PIV5 encodes two mRNA species through a process of pseudotemplated insertion of two G residues at a specific site during transcription, resulting in two viral proteins, V and P, whose N termini of 164 amino acid residues are identical. Previously it was reported that mutating six amino acid residues within this identical region results in a recombinant PIV5 (rPIV5-CPI؊) that exhibits elevated viral protein expression and induces production of cytokines, such as beta interferon and interleukin 6. Because the six mutations correspond to the shared region of the V protein and the P protein, it is not clear whether the phenotypes associated with rPIV5-CPI؊ are due to mutations in the P protein and/or mutations in the V protein. To address this question, we used a minigenome system and recombinant viruses to study the effects of mutations on the functions of the P and V proteins. We found that the P protein with six amino acid residue changes (Pcpi؊) was more efficient than wild-type P in facilitating replication of viral RNA, while the V protein with six amino acid residue changes (Vcpi؊) still inhibits minigenome replication as does the wild-type V protein. These results indicate that elevated viral gene expression in rPIV5-CPI؊ virus-infected cells can be attributed to a P protein with an increased ability to facilitate viral RNA synthesis. Furthermore, we found that a single amino acid residue change at position 157 of the P protein from Ser (the residue in the wild-type P protein) to Phe (the residue in Pcpi؊) is sufficient for elevated viral gene expression. Using mass spectrometry and 33 P labeling, we found that residue S157 of the P protein is phosphorylated. Based on these results, we propose that phosphorylation of the P protein at residue 157 plays an important role in regulating viral RNA replication.Parainfluenza virus 5 (PIV5), formerly known as simian virus 5, is a prototypical paramyxovirus in the Rubulavirus genus of Paramyxovirinae (4). The paramyxovirus family includes many important human and animal pathogens, such as Sendai virus, mumps virus, human parainfluenza viruses 1, 2, 3, and 4, Newcastle disease virus, measles virus, and emerging viruses, such as Hendra virus and Nipah virus (19). Paramyxoviruses contain nonsegmented negative-stranded RNA genomes, which are encapsidated by nucleocapsid protein (NP). The gene order within the paramyxovirus genomes is 3Ј-NP-P(V/W/C)-M-F-(SH)-HN-L-5Ј, where genes in parenthesis are not found in all species (reviewed in reference 19). The viral RNA-dependent RNA polymerase of paramyxoviruses minimally consists of two proteins, phosphoprotein (P) and the large (L) polymerase protein (11). The L proteins of paramyxoviruses have masses of 220 to 250 kDa. They have the capacity to initiate, elongate, and terminate transcription. In addition, they have the capacity to insert nontemplated G residues at selected sites within viral mRNAs during transcription and to add cap structures to t...

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“…Cells were cultured in 25 and 75cm 2 flasks and maintained in Eagle's MEM with Earle's salts, supplemented with 10% fetal calf serum and antibiotics as described [4]. The primary brain cell cultures were co-cultivated with African green monkey kidney (Veto) cells 12 (dog 1), 13 (dog 3), and 18 (dog 2) days after seeding.…”

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confidence: 99%

In vivo and in vitro expression of canine distemper viral proteins in dogs and non-domestic carnivores

Alldinger

Baumgärtner

Moll

et al. 1993

Archives of Virology

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The occurrence of the nucleo-, phospho-, matrix, fusion, and hemagglutinin proteins of the canine distemper virus (CDV) was investigated immunocytochemically in the brains of 3 dogs, 6 stone martens, 1 polecat, and 1 weasel. In addition, viral protein expression was studied in primary brain cell cultures of the 3 dogs after co-cultivation with Vero cells. Immunohistochemically, only minor differences, restricted to the H-4 epitope, were noted between the various species and CDV isolates. The data presented indicate that the mustelid virus is antigenically not distinct from the canine morbillivirus.

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Acute Encephalitis and Hydrocephalus in Dogs Caused by Canine Parainfluenza Virus

Cited by 44 publications

References 20 publications

Isolation and Characterization of Monoclonal Antibodies to Simian Virus 5 and Their Use in Revealing Antigenic Differences between Human, Canine and Simian Isolates

Isolation and Characterization of Monoclonal Antibodies to Simian Virus 5 and Their Use in Revealing Antigenic Differences between Human, Canine and Simian Isolates

A Single Amino Acid Residue Change in the P Protein of Parainfluenza Virus 5 Elevates Viral Gene Expression

In vivo and in vitro expression of canine distemper viral proteins in dogs and non-domestic carnivores

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