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Volume 78, Issue 11

Inhibition of pestivirus infection in cell culture by envelope proteins E(rns) and E2 of classical swine fever virus: E(rns) and E2 interact with different receptors. Free

Abstract

Pure preparations of envelope glycoproteins E and E2 of classical swine fever virus (CSFV) synthesized in insect cells were used to study infection of porcine and bovine cells with the pestiviruses CSFV and bovine viral diarrhoea virus (BVDV). Almost 100% inhibition of infection of porcine kidney cells with CSFV was produced by 100 μg/ml E. After removal of the virus no E was needed in the overlay medium (growth medium) to maintain this level of inhibition. In contrast, 100% inhibition of infection of porcine kidney cells with CSFV by 10 ^g/ml E2 was only achieved when E2 was added to the overlay medium. When E2 was omitted, a maximum of 50% inhibition was achieved. This indicated that after the virus and E2 were removed from the cells, infection still occurred, by virus particles which were still bound to the cell surface. Treatment with 100 μg/ml E released these particles from the cell surface. Furthermore, E bound irreversibly to the surface of cells susceptible or unsusceptible to pestivirus infection and cell-to-cell spread of CSFV was completely inhibited by E2 but not by E. These results demonstrated that E and E2 interacted with different cell surface receptors. Inhibition of BVDV infection of porcine and bovine cells by CSFV E2 suggested that CSFV E2 and BVDV E2 share an identical receptor. BVDV strain 5250 isolated from pigs was efficiently inhibited by CSFV E, whereas several BVDV strains isolated from cattle were not, suggesting that the conformation of E plays a role in host tropism.

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© Society for General Microbiology 1997
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1997-11-01
2024-04-25
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Inhibition of pestivirus infection in cell culture by envelope proteins E(rns) and E2 of classical swine fever virus: E(rns) and E2 interact with different receptors.
J. Gen. Virol. 78, 2779 (1997); https://doi.org/10.1099/0022-1317-78-11-2779
/content/journal/jgv/10.1099/0022-1317-78-11-2779
/content/journal/jgv/10.1099/0022-1317-78-11-2779
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