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

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 vi...

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Published inJournal of Integrative Agriculture Vol. 16; no. 5; pp. 1145 - 1152
Main Authors JING, Yan-chun, WU, Ying, SUN, Kun-feng, WANG, Ming-shu, CHENG, An-chun, CHEN, Shun, JIA, Ren-yong, ZHU, De-kang, LIU, Ma-feng, YANG, Qiao, JING, Bo, CHEN, Xiaoyue
Format Journal Article
LanguageEnglish
Published Key Laboratory of Animal Diseases and Human Health of Sichuan Province, Chengdu 611130, P.R.China 01.05.2017
Avian Diseases Research Center, Col ege of Veterinary Medicine, Sichuan Agricultural University, Chengdu 611130, P.R.China%Key Laboratory of Animal Diseases and Human Health of Sichuan Province, Chengdu 611130, P.R.China
KeAi Communications Co., Ltd
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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-AgC-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 HJTrapTM HeparJn 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-△gC-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.
AbstractList 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™ 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.
Many mammalian herpes viruses utilize heparan sulfate (HS) moieties present on cell surface proteoglycans as receptors for cellentry, 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 HiTrapTM 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 cel 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 cel s. This work provides us a foundation for further studies of examining the roles of gC in the adsorption during duck plague virus infection.
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-AgC-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 HJTrapTM HeparJn 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-△gC-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.
Author JING Yan-chun WU Ying SUN Kun-feng WANG Ming-shu CHENG An-chun CHEN Shun JIA Ren-yong ZHU De-kang LIU Ma-feng YANG Qiao JING Bo CHEN Xiao-yue
AuthorAffiliation Institute of Preventive Veterinary Medicine, Sichuan Agricultural University, Chengdu 611130, P.R.China Key Laboratory of Animal Diseases and Human Health of Sichuan Province, Chengdu 611130, P.R.China Avian Diseases Research Center, College of Veterinary Medicine, Sichuan Agricultural University, Chengdu 611130, P.R. China
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Keywords viral adsorption
glycoprotein C (gC)
heparan sulfate (HS)
duck plague virus (DPV)
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duck plague virus (DPV), glycoprotein C (gC), heparan sulfate (HS), viral adsorption
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-AgC-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 HJTrapTM HeparJn 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-△gC-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.
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Snippet Many mammalian herpes viruses utilize heparan sulfate (HS) moieties present on cell surface proteoglycans as receptors for cell entry, and this process also...
Many mammalian herpes viruses utilize heparan sulfate (HS) moieties present on cell surface proteoglycans as receptors for cell entry, and this process also...
Many mammalian herpes viruses utilize heparan sulfate (HS) moieties present on cell surface proteoglycans as receptors for cellentry, and this process also...
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SubjectTerms adsorption
Anatid alphaherpesvirus 1
chromatography
duck plague virus (DPV)
glycoprotein C (gC)
heparan sulfate
heparan sulfate (HS)
heparin
heparin lyase
mammals
mutants
proteoglycans
quantitative polymerase chain reaction
receptors
sulfates
viral adsorption
virulence
viruses
Title Role of duck plague virus glycoprotein C in viral adsorption: Absence of specific interactions with cell surface heparan sulfate
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Volume 16
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