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
Research output: Contribution to Journal/Magazine › Journal article › peer-review
}
TY - JOUR
T1 - The E2 glycoprotein is necessary but not sufficient for the adaptation of classical swine fever virus lapinized vaccine C-strain to the rabbit
AU - Li, Yongfeng
AU - Xie, Libao
AU - Zhang, Lingkai
AU - Wang, Xiao
AU - Li, Chao
AU - Han, Yuying
AU - Hu, Shouping
AU - Sun, Yuan
AU - Li, Su
AU - Luo, Yuzi
AU - Liu, Lihong
AU - Munir, Muhammad
AU - Qiu, Hua-Ji
N1 - 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
PY - 2018/6
Y1 - 2018/6
N2 - 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.
AB - 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.
KW - Classical swine fever virus
KW - C-strain
KW - E2 protein
KW - Adaptation
KW - Rabbit
U2 - 10.1016/j.virol.2018.04.016
DO - 10.1016/j.virol.2018.04.016
M3 - Journal article
C2 - 29734043
VL - 519
SP - 197
EP - 206
JO - Virology
JF - Virology
SN - 0042-6822
ER -