The E2 glycoprotein is necessary but not sufficient for the adaptation of classical swine fever virus lapinized vaccine C-strain to the rabbit

Abstract

Classical swine fever virus (CSFV) C-strain was developed through hundreds of passages of a highly virulent CSFV in rabbits. To investigate the molecular basis for the adaptation of C-strain to the rabbit (ACR), a panel of chimeric viruses with the exchange of glycoproteins E^rns, E1, and/or E2 between C-strain and the highly virulent Shimen strain and a number of mutant viruses with different amino acid substitutions in E2 protein were generated and evaluated in rabbits. Our results demonstrate that Shimen-based chimeras expressing E^rns-E1-E2, E^rns-E2 or E1-E2 but not E^rns-E1, E^rns, E1, or E2 of C-strain can replicate in rabbits, indicating that E2 in combination with either E^rns or E1 confers the ACR. Notably, E2 and the amino acids P108 and T109 in Domain I of E2 are critical in ACR. Collectively, our data indicate that E2 is crucial in mediating the ACR, which requires synergistic contribution of E^rns or E1.

Keywords: Adaptation; C-strain; Classical swine fever virus; E2 protein; Rabbit.