Abstract
Rotavirus D (RV-D) is gaining importance as a cause of gastroenteritis and runting and stunting syndrome (RSS) in poultry. To date, information is scarce on the molecular analysis of RV-D isolates worldwide. In this study, the VP7 gene, a major constituent of outer capsid structural protein, from a RV-D isolate (UKD48) obtained from Uttarakhand state was analyzed. Phylogenetically, the RV-D isolate was found to be closely related to a South Korean strain, and the nucleotide percent identity varied from 80.4–84.2% with other RV-D strains available globally. Furthermore, domain investigation within 21 aligned amino acid sequences of the VP7 gene affirmed that this gene has several domains: a conserved glycosylation site (N–I–T) having an important role in protein folding; a N-terminal signal peptide (“ITG”) for endoplasmic reticulum retention; and two hydrophobic sites for elucidating transmembrane portions, antigenic structures, and so forth. The findings suggest that the VP7 gene of the Indian RV-D isolate is genetically distinct from those of other avian RV-Ds. Although biological evidence is still needed to prove the functional characteristics of these domains in outer capsid structural proteins, the present study adds new knowledge and derives the need for further investigation.
Highlights
Rotaviruses (RVs) have been identified as one of the main etiological agents of diarrhea and enteritis in mammals, including humans and avian species [1,2]
Studies have proven the importance of glycosylation and hydrophobic/hydrophilic domains in protein folding, and the presence of the
The sample from the intestinal scraping collected from a young layer chick (UKD48) exhibiting signs of severe enteritis was confirmed for the presence of Rotavirus D (RV-D) using VP6 gene-based RT-PCR, yielding an expected amplicon of 185 bp (Figure 1A)
Summary
Rotaviruses (RVs) have been identified as one of the main etiological agents of diarrhea and enteritis in mammals, including humans and avian species [1,2]. Studies have proven the importance of glycosylation and hydrophobic/hydrophilic domains in protein folding, and the presence of the Pathogens 2018, 7, 37 highlights the genetic relatedness of the VP7 gene of an RV-D isolate (UKD48) to other RV-D strains, N-glycosylation sites, distribution of hydrophobic/hydrophilic domains, and defines N-terminal signal peptide domains within the target gene sequences.
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