Role of duck plague virus glycoprotein C in viral adsorption: Absence of specific interactions with cell surface heparan sulfate

Abstract

Many mammalian herpes viruses utilize heparan sulfate (HS) moieties present on cell surface proteoglycans as receptors for cell entry, and this process also requires viral glycoprotein C (gC) homologues. However, our understanding of the role of gC in facilitating attachment of other alpha-herpes viruses such as the duck plague virus (DPV) remains preliminary. To study the role of gC during DPV infection, we used a gC-deleted mutant virus (DPV-ΔgC-EGFP). Examination of the viral copy number by real-time PCR, as well as time course studies of viral adsorption and proliferation revealed that gC was involved in the viral binding to the cell surface. The affinity of viral glycoproteins (gB-DPV, gC-DPV, and gE-DPV) to HS was assessed using a prokaryotic expression system and HiTrap TM Heparin HP column chromatography. In addition, to confirm that gC played a role in the interaction between DPV and HS, viruses were treated with the HS analogue heparin and host cells were treated with its inhibitors heparinase prior to exposure to DPV-ΔgC-EGFP or wild-type strain Chinese virulent duck plague virus (DPV-CHv). The effects of heparin and heparinase on virus infectivity demonstrated that function of gC on viral adsorption is independent of interactions between gC and heparin sulfate on cell surface. All in all, this study demonstrated that the gC of DPV can mediate viral adsorption in an HS-independent manner, which distinguish it from the gC of some other alpha-herpes viruses. Future studies will be required to identify the receptors involved in gC protein binding to cells. This work provides us a foundation for further studies of examining the roles of gC in the adsorption during duck plague virus infection.

Duck plague virus Glycoprotein J is functional but slightly impaired in viral replication and cell-to-cell spread

“…However, previously studies about DPV focused on the epidemiology and prevention, instead of the studying of molecular biology and the function of glycoproteins 5 . To date only a few gens such as gC and gE from DPV have been addressed by studying mutant viruses 12 , 13 . gC involved in alphaherpesvirus adsorption were present in the DPV genome and relatively conserved, but the function of DPV gC also makes a difference with other alphaherpesvirus, which is independent of interaction with heparin sulfate of cell surface 12 , 14 .…”

“…To date only a few gens such as gC and gE from DPV have been addressed by studying mutant viruses 12 , 13 . gC involved in alphaherpesvirus adsorption were present in the DPV genome and relatively conserved, but the function of DPV gC also makes a difference with other alphaherpesvirus, which is independent of interaction with heparin sulfate of cell surface 12 , 14 . Therefore, although alphaherpesvirus share many common strategies for their replication cycle 15 , they also keep some individually patterns to invade and infect target cells.…”

Two nuclear localization signals regulate intracellular localization of the Duck enteritis virus UL13 protein

“…The target segment (UL13 left arm-FRT-Kan-FRT-UL14 right arm) was PCR-amplified using the ΔUL13&UL14 F F/R primers (Table 2). Then, the infectious clone DEV CHv-ΔUL13&UL14-G was generated by employing a recombinating system based on the genetic manipulation of the DEV CHv-G infectious clone [34][35][36][37]. Briefly, the pKD46 plasmid, which encodes the recombination genes exo, beta, and gam under the tight control of a ParaB promoter, was first introduced into E. coli DH10B containing the DEV CHv-G plasmid by electrophoretic transfer.…”

Duck enteritis virus pUL47, as a late structural protein localized in the nucleus, mainly depends on residues 40 to 50 and 768 to 777 and inhibits IFN-β signalling by interacting with STAT1

“…The properties of some DEV genes have been preliminary characterized [21][22][23][24][25][26][27][28][29][30][31][32][33][34][35][36]. We previously reported that DEV UL47-encoded protein (pUL47) modulates the distribution of UL41-encoded protein (pUL41) [37].…”