First Molecular Evidence and Genetic Characterization of Ovine Herpesvirus 2 in Multiple Animal Species in India
Autor: | Vijendra Pal Singh, R. Ramprabhu, Richa Sood, Sandeep Bhatia, A. K. Pateriya, Roma Dixit, E. Venkatesakumar, Naveen Kumar |
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Jazyk: | angličtina |
Rok vydání: | 2021 |
Předmět: |
040301 veterinary sciences
India Molecular evidence ovine herpesvirus 2 malignant catarrhal fever 0403 veterinary science 03 medical and health sciences Capra hircus Glycoprotein B glycoprotein B Ovis Gene 030304 developmental biology chemistry.chemical_classification Genetics 0303 health sciences lcsh:Veterinary medicine biology Phylogenetic tree General Veterinary multiple animals species 04 agricultural and veterinary sciences Brief Research Report biology.organism_classification Ovine herpesvirus 2 Amino acid chemistry lcsh:SF600-1100 Veterinary Science |
Zdroj: | Frontiers in Veterinary Science Frontiers in Veterinary Science, Vol 8 (2021) |
ISSN: | 2297-1769 |
DOI: | 10.3389/fvets.2021.610178 |
Popis: | Ovine herpesvirus 2 (OvHV-2) is the causative agent of sheep-associated malignant catarrhal fever (SA-MCF), a highly fatal disease syndrome that predominantly affects susceptible hosts of the order Artiodactyla. In this study, an in-depth clinico-molecular investigation of SA-MCF disease in a morbid 50-days-old cattle calf (Bos taurus indicus) and asymptomatic infection in the in-contact reservoir hosts, sheep (Ovis aries), and goat (Capra hircus) housed on a farm located in the Southern India is reported. An OIE recommended SA-MCF type-specific PCR confirmed the etiological agent as OvHV-2. The genetic characterization and phylogenetic analyses based on the glycoprotein B (gB) gene indicate that three genetic variants of OvHV-2 had infected the animal cluster of this study. As the OvHV-2 infection eventually lead to the death of the cattle calf, and the fact that its gB sequence carried four unique amino acid substitutions (N169S, L594P, I645V, and V730A), an investigation of these substitutions impact on its stability and molecular flexibility was carried out. The mapping of these amino acid substitutions on the three-dimensional structure of gB coupled with supplementary investigations showed that these substitutions conveyed the molecular flexibility to the gB, at the cost of its stability. Future studies would be to investigate whether these gB substitutions have any impact on membrane fusion activity using a virus-free cell-to-cell membrane fusion assay. The study also highlights the importance of adopting stringent biosecurity measures where mixed animal farming is a common practice. |
Databáze: | OpenAIRE |
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