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Significance of the oligosaccharides of the porcine reproductive and respiratory syndrome virus glycoproteins GP_2a and GP₅ for infectious virus production

E. H. J. Wissink^1,

J. J. M. Meulenberg^1,

P. A. van Rijn^1,

¹ Animal Sciences Group, Wageningen University, Division of Infectious Diseases, Edelhertweg 15, PO Box 65, 8200 AB Lelystad, The Netherlands
² Virology Division, Utrecht University, Utrecht, The Netherlands

Correspondence
F. A. M. Rijsewijk
frans.rijsewijk{at}wur.nl

The arterivirus porcine reproductive and respiratory syndrome virus (PRRSV) contains four glycoproteins, GP_2a, GP₃, GP₄ and GP₅, the functions of which are still largely unresolved. In this study, the significance of the N-glycosylation of the GP_2a and GP₅ proteins of PRRSV strain LV was investigated. Both glycoproteins contain two predicted N-glycosylation sites that are highly conserved between North American-type and European-type PRRSV. Using site-directed mutagenesis, single and double mutant full-length PRRSV cDNA clones were generated. After analysing the expression of the mutant proteins and the actual use of the four putative glycosylation sites in the wild-type proteins, the production of mutant virus particles and their infectivities were investigated. The results showed that the N-linked glycans normally present on the GP_2a protein are not essential for particle formation, as is the oligosaccharide attached to N53 of the GP₅ protein. In contrast, the oligosaccharide linked to N46 of the GP₅ protein is strongly required for virus particle production. The specific infectivities of the mutant viruses were investigated by comparing their infectivity-per-particle ratios with that of wild-type virus. The results showed that the lack of either one or both of the N-linked oligosaccharides on GP_2a or of the oligosaccharide attached to N53 of GP₅ did not significantly affect the infectivities of the viruses. In contrast, the two recombinant viruses lacking the oligosaccharide bound to N46 exhibited a significantly reduced specific infectivity compared with the wild-type virus. The implications of the differential requirements of the modifications of GP_2a and GP₅ for PRRSV assembly and infectivity are discussed.

Present address: Netherlands Cancer Institute (NKI/AvL), Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands.

Present address: Amsterdam Molecular Therapeutics (AMT), Meibergdreef 61, PO Box 22506, 1105 DA Amsterdam, The Netherlands.

Present address: Central Institute for Animal Disease Control (CIDC-Lelystad), Houtribweg 39, PO Box 2004, 8203 AA Lelystad, The Netherlands.

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