Isolation, characterization, and pathogenicity studies of a bovine respiratory syncytial virus

Smith, Malcolm Herbert

doi:10.31274/rtd-180816-3342

Cited by 16 publications

(21 citation statements)

References 20 publications

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“…BRSV infections can be diagnosed by virus isolation or serology. However, since BRSV is labile, virus isolation fails on many occasions [14,18]. Among serological methods, ELISA is highly sensitive and rapid.…”

Section: Discussionmentioning

confidence: 99%

Bovine respiratory syncytial virus: first serological evidence in Uruguay

et al. 2000

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-Bovine respiratory syncytial virus (BRSV) is a major cause of respiratory disease in calves resulting in a substantial economic loss for the cattle industry worldwide. In order to determine the presence of BRSV in Uruguay, an immunoenzymatic test was set up, using a recombinant BRSV nucleocapsid (N) protein as the antigen. The N protein was produced in Sf9 insect cells by a recombinant baculovirus expressing the N protein. Serum samples collected from one hundred cattle from four different geographic regions of Uruguay were analyzed. Antibodies against the N protein of BRSV were detected in 95% of the serum samples analyzed. These results show for the first time the presence of BRSV antibodies and suggest a widespread BRSV infection in the cattle population of Uruguay. respiratory syncytial virus / recombinant N protein / epidemiology / baculovirus / UruguayRésumé -Première mise en évidence sérologique du virus syncytial respiratoire bovin en Uruguay. Le virus syncytial respiratoire bovin (VSRB) est une cause majeure de maladie respiratoire chez le veau, provoquant des pertes économiques importantes pour l'industrie bovine dans le monde entier. Afin de mettre en évidence la présence du VSRB en Uruguay, un test immunoenzymatique a été élaboré, qui utilise comme antigène une protéine recombinante de nucléocapside (N) du VSRB. La protéine N a été produite dans des cellules d'insecte Sf9 par un baculovirus recombinant exprimant la protéine N. Des échantillons de sérum prélevés sur 100 bovins, provenant de quatre régions différentes d'Uruguay, ont été analysés. Des anticorps dirigés contre la protéine N du VSRB ont été détectés dans 95% des échantillons analysés. Ces résultats montrent, pour la première fois, la présence d'anticorps anti-VSRB et suggèrent que l'infection par le VSRB est largement répandue dans la population bovine en Uruguay. virus syncytial respiratoire bovin / protéine N recombinante / épidémiologie / baculovirus / Uruguay Vet. Res. 31 (2000) [241][242][243][244][245][246] 241

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Section: Discussionmentioning

confidence: 99%

Bovine respiratory syncytial virus: first serological evidence in Uruguay

et al. 2000

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“…1,4,11,13,14,29,30 Ruminant RSV isolates include viruses from cattle, sheep, and goats suffering from lower respiratory tract infection. 5,17,18,27 Bovine RSV is a major cause of respiratory disease in cattle and shares many similarities with human RSV with respect to epidemiologic patterns, clinical disease, immunologic response, and pathologic features. 5,17 Severe infections occur at a young age, and infections can also occur in the presence of passively-derived immunity.…”

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Analysis of Ruminant Respiratory Syncytial Virus Isolates by RNAse Protection of the G Glycoprotein Transcripts

et al. 1999

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Abstract. Two different respiratory syncytial virus (RSV) radiolabeled probes were used to characterize the genetic heterogeneity of 25 ruminant RSV isolates by the ribonuclease protection assay. A 32 P-radiolabeled antisense RNA probe was transcribed from cloned ovine and bovine RSV G glycoprotein genes and then hybridized with total RNA isolated from infected cells with various ruminant RSV isolates. The results of this study, along with previously published nucleotide sequence data of the ovine RSV G glycoprotein gene, suggest the presence of at least 2 ruminant RSV subgroups. One subgroup is represented by RSV isolated from respiratory disease outbreaks from calves and goats, and the other is represented by RSV isolated from sheep.

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“…To examine the sequence homology between P mRNA sequences of two strains of BRSV, a cDNA library was established from mRNA isolated from MDBK cells infected with the FS-1 strain of BRSV (Smith et al, 1975) as described previously . The cDNA clones for the P mRNA were selected by crosshybridization, and two independent clones containing sequence from nucleotide 23 to the end of the mRNA were sequenced.…”

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Sequence comparison between the phosphoprotein mRNAs of human and bovine respiratory syncytial viruses identifies a divergent domain in the predicted protein

Mallipeddi

Samal

1992

Journal of General Virology

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The nucleotide and deduced amino acid sequences of the phosphoprotein (P) mRNA of bovine respiratory syncytial virus (BRSV) strain A51908 have been determined. The P mRNA is 860 nucleotides long with a single large open reading frame and the encoded polypeptide is 241 amino acids long. Comparison with the corresponding sequences of human respiratory syncytial virus (HRSV) subgroups A and B revealed 72 to 74% identity at the nucleotide level, and 81% at the amino acid level. The P protein contains a single divergent domain (37 % amino acid identity) flanked by highly conserved domains (87 % amino acid identity). The 3' end non-coding region is 47 nucleotides shorter than the corresponding region of HRSV. Comparison of the P mRNA sequences of two strains of BRSV (A51908 and FS-1) showed that there was extensive sequence identity at both the nucleotide (97%) and amino acid (97-9%) levels.

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Isolation, characterization, and pathogenicity studies of a bovine respiratory syncytial virus

Cited by 16 publications

References 20 publications

Bovine respiratory syncytial virus: first serological evidence in Uruguay

Bovine respiratory syncytial virus: first serological evidence in Uruguay

Analysis of Ruminant Respiratory Syncytial Virus Isolates by RNAse Protection of the G Glycoprotein Transcripts

Sequence comparison between the phosphoprotein mRNAs of human and bovine respiratory syncytial viruses identifies a divergent domain in the predicted protein

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