Rights statement: This is the author’s version of a work that was accepted for publication in Virology. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Virology, 519, 2018 DOI: 10.1016/j.virol.2018.04.016
Accepted author manuscript, 6.66 MB, PDF document
Available under license: CC BY-NC-ND
Final published version
Research output: Contribution to Journal/Magazine › Journal article › peer-review
| <mark>Journal publication date</mark> | 06/2018 |
|---|---|
| <mark>Journal</mark> | Virology |
| Volume | 519 |
| Number of pages | 10 |
| Pages (from-to) | 197-206 |
| Publication Status | Published |
| Early online date | 7/05/18 |
| <mark>Original language</mark> | English |
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 Erns, 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 Erns-E1-E2, Erns-E2 or E1-E2 but not Erns-E1, Erns, E1, or E2 of C-strain can replicate in rabbits, indicating that E2 in combination with either Erns 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 Erns or E1.