Abstract
The major neutralizing epitope of porcine reproductive and respiratory syndrome virus (PRRSV) is mainly located on virus glycoprotein 5 (GP5). Immunization with exogenous GP5 or exposure to native GP5 by means of DNA immunization can provide some degree of immune protection to PRRSV infection in pigs. However, during PRRSV infection in pigs, the production of neutralization antibodies induced by GP5 is delayed or suppressed. This suggests that the synthesis of GP5 is late than some PRRSV proteins or other PRRSV proteins interfering with the function of GP5 in inducing host responses during virus infection. Here, to exclude the impacts of the other PRRSV proteins and determine the role of GP5 in the replication of PRRSV in vitro, a Marc-145 cell line stably expressing GP5 (Marc-145-GP5Flag) was constructed. Cell proliferation and cell apoptosis measurements indicated that the expression of GP5 in Marc-145 cells did not disturb the cells’ viability. Following infection with different PRRSV strains PRRSV replication in Marc-145-GP5Flag cells was inhibited significantly. Type I interferon assay results showed that beta interferon (IFN-β) in the Marc-145-GP5Flag cells were increased at mRNA and protein levels. When siRNA was introduced into the cells to knock down IFN-β mRNA, PRRSV infectivity of these cells was recovered. These data suggest that early GP5 expression is not favorable for further infection by PRRSV, because it not only stimulates production of neutralization antibodies in pigs, but also induces IFN-β production in host cells. Therefore, GP5 is an important protein in the induction of self-protection responses from the host.
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