A triple amino acid substitution at position 88/94/95 in glycoprotein GP2a of type 1 porcine reproductive and respiratory syndrome virus (PRRSV1) is responsible for adaptation to MARC-145 cells
- Author
- Jiexiong Xie (UGent) , Ivan Trus (UGent) , Dayoung Oh (UGent) , Lise K Kvisgaard, Julie CF Rappe, Nicolas Ruggli, Nathalie Vanderheijden (UGent) , Lars E Larsen, François Lefèvre and Hans Nauwynck (UGent)
- Organization
- Abstract
- The Meat Animal Research Center-145 (MARC-145) cell line has been proven to be valuable for viral attenuation regarding vaccine development and production. Cell-adaptation is necessary for the efficient replication of porcine reproductive and respiratory syndrome virus (PRRSV) in these cells. Multiple sequence analysis revealed consistent amino acid substitutions in GP2a (V88F, M94I, F95L) of MARC-145 cell-adapted strains. To investigate the putative effect of these substitutions, mutations at either position 88, 94, 95, and their combinations were introduced into two PRRSV1 (13V091 and IVI-1173) infectious clones followed by the recovery of viable recombinants. When comparing the replication kinetics in MARC-145 cells, a strongly positive effect on the growth characteristics of the 13V091 strain (+2.1 log10) and the IVI-1173 strain (+1.7 log10) compared to wild-type (WT) virus was only observed upon triple amino acid substitution at positions 88 (V88F), 94 (M94I), and 95 (F95L) of GP2a, suggesting that the triple mutation is a determining factor in PRRSV1 adaptation to MARC-145 cells.
- Keywords
- PRRSV, GP2a, MARC-145, adaptation mutation, MINOR ENVELOPE PROTEINS, DENDRITIC CELLS, MUTATION-RATES, REPLICATION, IDENTIFICATION, RECEPTOR, STRAINS, SUSCEPTIBILITY, NIDOVIRALES, INVOLVEMENT
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Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-8598769
- MLA
- Xie, Jiexiong, et al. “A Triple Amino Acid Substitution at Position 88/94/95 in Glycoprotein GP2a of Type 1 Porcine Reproductive and Respiratory Syndrome Virus (PRRSV1) Is Responsible for Adaptation to MARC-145 Cells.” VIRUSES, vol. 11, no. 1, 2019.
- APA
- Xie, J., Trus, I., Oh, D., Kvisgaard, L. K., Rappe, J. C., Ruggli, N., … Nauwynck, H. (2019). A triple amino acid substitution at position 88/94/95 in glycoprotein GP2a of type 1 porcine reproductive and respiratory syndrome virus (PRRSV1) is responsible for adaptation to MARC-145 cells. VIRUSES, 11(1).
- Chicago author-date
- Xie, Jiexiong, Ivan Trus, Dayoung Oh, Lise K Kvisgaard, Julie CF Rappe, Nicolas Ruggli, Nathalie Vanderheijden, Lars E Larsen, François Lefèvre, and Hans Nauwynck. 2019. “A Triple Amino Acid Substitution at Position 88/94/95 in Glycoprotein GP2a of Type 1 Porcine Reproductive and Respiratory Syndrome Virus (PRRSV1) Is Responsible for Adaptation to MARC-145 Cells.” VIRUSES 11 (1).
- Chicago author-date (all authors)
- Xie, Jiexiong, Ivan Trus, Dayoung Oh, Lise K Kvisgaard, Julie CF Rappe, Nicolas Ruggli, Nathalie Vanderheijden, Lars E Larsen, François Lefèvre, and Hans Nauwynck. 2019. “A Triple Amino Acid Substitution at Position 88/94/95 in Glycoprotein GP2a of Type 1 Porcine Reproductive and Respiratory Syndrome Virus (PRRSV1) Is Responsible for Adaptation to MARC-145 Cells.” VIRUSES 11 (1).
- Vancouver
- 1.Xie J, Trus I, Oh D, Kvisgaard LK, Rappe JC, Ruggli N, et al. A triple amino acid substitution at position 88/94/95 in glycoprotein GP2a of type 1 porcine reproductive and respiratory syndrome virus (PRRSV1) is responsible for adaptation to MARC-145 cells. VIRUSES. 2019;11(1).
- IEEE
- [1]J. Xie et al., “A triple amino acid substitution at position 88/94/95 in glycoprotein GP2a of type 1 porcine reproductive and respiratory syndrome virus (PRRSV1) is responsible for adaptation to MARC-145 cells,” VIRUSES, vol. 11, no. 1, 2019.
@article{8598769,
abstract = {The Meat Animal Research Center-145 (MARC-145) cell line has been proven to be valuable for viral attenuation regarding vaccine development and production. Cell-adaptation is necessary for the efficient replication of porcine reproductive and respiratory syndrome virus (PRRSV) in these cells. Multiple sequence analysis revealed consistent amino acid substitutions in GP2a (V88F, M94I, F95L) of MARC-145 cell-adapted strains. To investigate the putative effect of these substitutions, mutations at either position 88, 94, 95, and their combinations were introduced into two PRRSV1 (13V091 and IVI-1173) infectious clones followed by the recovery of viable recombinants. When comparing the replication kinetics in MARC-145 cells, a strongly positive effect on the growth characteristics of the 13V091 strain (+2.1 log10) and the IVI-1173 strain (+1.7 log10) compared to wild-type (WT) virus was only observed upon triple amino acid substitution at positions 88 (V88F), 94 (M94I), and 95 (F95L) of GP2a, suggesting that the triple mutation is a determining factor in PRRSV1 adaptation to MARC-145 cells.},
articleno = {36},
author = {Xie, Jiexiong and Trus, Ivan and Oh, Dayoung and Kvisgaard, Lise K and Rappe, Julie CF and Ruggli, Nicolas and Vanderheijden, Nathalie and Larsen, Lars E and Lefèvre, François and Nauwynck, Hans},
issn = {1999-4915},
journal = {VIRUSES},
keywords = {PRRSV,GP2a,MARC-145,adaptation mutation,MINOR ENVELOPE PROTEINS,DENDRITIC CELLS,MUTATION-RATES,REPLICATION,IDENTIFICATION,RECEPTOR,STRAINS,SUSCEPTIBILITY,NIDOVIRALES,INVOLVEMENT},
language = {eng},
number = {1},
pages = {17},
title = {A triple amino acid substitution at position 88/94/95 in glycoprotein GP2a of type 1 porcine reproductive and respiratory syndrome virus (PRRSV1) is responsible for adaptation to MARC-145 cells},
url = {http://dx.doi.org/10.3390/v11010036},
volume = {11},
year = {2019},
}
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