Abstract

A short alternative open reading frame named ORF7a has recently been discovered within the nucleocapsid gene of the porcine reproductive and respiratory syndrome virus (PRRSV) genome. Proteins (7ap) translated from the ORF7a of two divergent strains - a type I and a type II - are able to completely reduce the motility of nucleic acids at relatively high molar charge ratios in gel retardation assays indicating strong dsDNA-and ssRNA-binding capability. Conserved RNA-and DNA-binding properties suggest that nucleic acid binding is a functional property of the divergent 7aps, and not an arbitrary consequence of their net positive charge. Sera from Hu7ap-immunised pigs and mice did not react with Hu7ap or Hu7ap-GFP; however, antinuclear antibodies were detected in the sera of the immunised animals, suggesting an ability of Hu7ap to interact with or mimic autoantigenic macromolecules.

Keywords

Porcine reproductive and respiratory syndrome virus; ORF7a; 7ap proteins; nucleic acid binding features; antinuclear antibodies

Published in

Acta Veterinaria Hungarica
2017, Volume: 65, number: 1, pages: 124-134
Publisher: AKADEMIAI KIADO RT

SLU Authors

• Belak, Sandor

  • Department of Animal Biosciences, Swedish University of Agricultural Sciences
    

UKÄ Subject classification

Medical Bioscience


Publication identifier

DOI: https://doi.org/10.1556/004.2017.013

Permanent link to this page (URI)

https://res.slu.se/id/publ/91844