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...
Saved in:
Published in | Journal of Integrative Agriculture Vol. 16; no. 5; pp. 1145 - 1152 |
---|---|
Main Authors | , , , , , , , , , , , |
Format | Journal Article |
Language | English |
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 |
Subjects | |
Online Access | Get full text |
Cover
Loading…
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 |
AuthorAffiliation_xml | – name: Key Laboratory of Animal Diseases and Human Health of Sichuan Province, Chengdu 611130, P.R.China;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 |
Author_xml | – sequence: 1 givenname: Yan-chun surname: JING fullname: JING, Yan-chun – sequence: 2 givenname: Ying surname: WU fullname: WU, Ying – sequence: 3 givenname: Kun-feng surname: SUN fullname: SUN, Kun-feng – sequence: 4 givenname: Ming-shu surname: WANG fullname: WANG, Ming-shu – sequence: 5 givenname: An-chun surname: CHENG fullname: CHENG, An-chun – sequence: 6 givenname: Shun surname: CHEN fullname: CHEN, Shun – sequence: 7 givenname: Ren-yong surname: JIA fullname: JIA, Ren-yong – sequence: 8 givenname: De-kang surname: ZHU fullname: ZHU, De-kang – sequence: 9 givenname: Ma-feng surname: LIU fullname: LIU, Ma-feng – sequence: 10 givenname: Qiao surname: YANG fullname: YANG, Qiao – sequence: 11 givenname: Bo surname: JING fullname: JING, Bo – sequence: 12 givenname: Xiaoyue surname: CHEN fullname: CHEN, Xiaoyue |
BookMark | eNqFkc1u1DAQxyNUJErpIyBZnNpDwHZiZyNO1YqPSpWQ-DhbE2ec9Ta1U9uhLEceg2fhnXgFnN2WAxcutmf0m_-M5_-0OHLeYVE8Z_Qlo0y--sRpK8qKsfaMyXPJhKAlf1Qc80rwsqq5OMrvB-RJcRrjllK6YFSujosfH_2IxBvSz_qaTCMMM5KvNsyRDONO-yn4hNaRNclHzsNIoI8-TMl69_vXT3LRRXR6LxEn1NZYndGEAfSCRHJn04ZoHEcS52AgoxucIIDL8Wgg4bPisYEx4un9fVJ8efvm8_p9efXh3eX64qrUtaSpBFl1rWFNr3vemq7tK6HrlahbCSvGGW2wrlCwBoXWHaxkVzPBeG-kbhvW0FV1UlwedHsPWzUFewNhpzxYtU_4MCgIyeoRFQisekPBaAM1mqbDvhGyM5IidkBp1jo_aN2BM-AGtfVzcHl69X1wu-tvCjnNTQVlbWbPDmze5e2MMakbG5eFgEM_R8WzH3VT0XpBxQHVwccY0Pwdk1G12K32dqvFS5Wjvd2K57rX_9Rpm2DZfwpgx_9Wv7iv3ng33Nr8nYe2suG04W1Nqz85X8CP |
CitedBy_id | crossref_primary_10_1186_s13567_020_00859_w crossref_primary_10_1038_s41598_018_34503_7 crossref_primary_10_1155_2020_9630452 crossref_primary_10_1016_S2095_3119_20_63175_6 crossref_primary_10_1038_s41598_018_22447_x |
Cites_doi | 10.1006/viro.2001.1326 10.1016/S0168-1702(97)00149-4 10.1292/jvms.63.427 10.1128/JVI.01517-12 10.1016/j.virusres.2013.01.015 10.1186/1743-422X-8-214 10.1128/JVI.00529-12 10.1016/B978-0-12-800269-8.00003-8 10.1016/S0042-6822(03)00166-1 10.1128/JVI.74.19.9106-9114.2000 10.1128/mBio.00046-13 10.1016/j.antiviral.2003.12.007 10.1186/1743-422X-7-37 10.1186/1743-422X-10-89 10.1007/s007050070039 10.1016/j.virol.2003.09.029 10.1128/JVI.75.22.11137-11145.2001 10.1006/viro.1999.9609 10.1006/viro.1995.9957 10.1016/j.bbrc.2009.11.027 10.1016/j.virol.2003.10.004 10.1016/j.ab.2014.11.007 10.1099/vir.0.19641-0 10.1016/j.virusres.2011.07.004 10.2307/1592999 10.1016/S0300-9084(01)01290-1 10.1016/j.virol.2007.11.014 10.2174/1874357901307010005 10.4238/2014.June.17.2 10.1099/vir.0.016634-0 10.1016/B978-0-12-800269-8.00008-7 10.1016/S0042-6822(02)00024-7 10.1016/j.virol.2005.09.016 10.1128/JVI.00908-12 10.1186/1743-422X-7-349 10.1186/1743-422X-7-120 10.1016/0168-1702(95)01277-X 10.1016/j.virusres.2010.03.003 10.1128/JVI.62.8.2850-2858.1988 |
ContentType | Journal Article |
Copyright | Copyright © Wanfang Data Co. Ltd. All Rights Reserved. |
Copyright_xml | – notice: Copyright © Wanfang Data Co. Ltd. All Rights Reserved. |
DBID | 2RA 92L CQIGP W95 ~WA AAYXX CITATION 7S9 L.6 2B. 4A8 92I 93N PSX TCJ DOA |
DOI | 10.1016/S2095-3119(16)61550-2 |
DatabaseName | 维普期刊资源整合服务平台 中文科技期刊数据库-CALIS站点 中文科技期刊数据库-7.0平台 中文科技期刊数据库-农业科学 中文科技期刊数据库- 镜像站点 CrossRef AGRICOLA AGRICOLA - Academic Wanfang Data Journals - Hong Kong WANFANG Data Centre Wanfang Data Journals 万方数据期刊 - 香港版 China Online Journals (COJ) China Online Journals (COJ) DOAJ Directory of Open Access Journals |
DatabaseTitle | CrossRef AGRICOLA AGRICOLA - Academic |
DatabaseTitleList | AGRICOLA |
Database_xml | – sequence: 1 dbid: DOA name: DOAJ Directory of Open Access Journals url: https://www.doaj.org/ sourceTypes: Open Website |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Agriculture |
DocumentTitleAlternate | Role of duck plague virus glycoprotein C in viral adsorption: Absence of specific interactions with cell surface heparan sulfate |
EISSN | 2352-3425 |
EndPage | 1152 |
ExternalDocumentID | oai_doaj_org_article_a5e3df0afcfa4ef7bed756bf60eeba00 zgnykx_e201705019 10_1016_S2095_3119_16_61550_2 672072940 |
GrantInformation_xml | – fundername: the grants from the National Natural Science Foundation of China; the Na-tional Key Technologies R&D Program of China during the 12th Five-Year Plan period; the Founda-tion of China Agricultural Research System; the Major Project of Education Department in Sichuan, China funderid: (31072157); (2015BAD12B05); (CARS-43-8); (16ZA0027) |
GroupedDBID | --M -04 -0D -SD -S~ .~1 0R~ 1B1 1~. 1~5 2B. 2B~ 2RA 4.4 457 4G. 5VR 7-5 8P~ 92G 92I 92L 92M 93N 93Q 9D9 9DD AABNK AABVA AACTN AAEDT AAEDW AAIAV AAIKJ AAKOC AALRI AAOAW AATLK AAXUO ABGRD ABMAC ABXDB ABYKQ ACDAQ ACGFS ACRLP ADEZE ADMUD ADQTV AEBSH AEKER AENEX AEQOU AFKWA AFTJW AFUIB AFXIZ AGHFR AGUBO AGYEJ AIEXJ AIKHN AITUG AJBFU AJOXV ALMA_UNASSIGNED_HOLDINGS AMFUW AMRAJ AXJTR BKOJK BLXMC CAJED CAJUS CBWCG CCEZO CHDYS CQIGP EBS EFJIC EFLBG EJD FA0 FDB FIRID FNPLU FYGXN GBLVA GROUPED_DOAJ HZ~ JUIAU KOM M41 MO0 NCXOZ O-L O9- OAUVE OK1 P-8 P-9 PC. Q-- Q-3 Q38 R-D RIG ROL RT4 SDF SDG SES SSA SSZ T5K T8T TCJ TGD U1F U1G U5D U5N W95 ~G- ~WA AAHBH AATTM AAXKI AAYWO AAYXX ABJNI ABWVN ACRPL ACVFH ADCNI ADNMO ADVLN AEIPS AEUPX AFJKZ AFPUW AGCQF AGRNS AIGII AIIUN AKBMS AKRWK AKYEP ANKPU APXCP BNPGV CITATION SSH 7S9 L.6 4A8 PSX EFKBS |
ID | FETCH-LOGICAL-c460t-a63b9f17dcd29fb9d35c485496a812107e43e517e5ccba86b41512df6c9717083 |
IEDL.DBID | DOA |
ISSN | 2095-3119 |
IngestDate | Wed Aug 27 01:16:25 EDT 2025 Thu May 29 03:54:11 EDT 2025 Fri Jul 11 16:34:59 EDT 2025 Tue Jul 01 01:08:40 EDT 2025 Thu Apr 24 23:08:41 EDT 2025 Wed Feb 14 10:01:46 EST 2024 |
IsDoiOpenAccess | true |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 5 |
Keywords | viral adsorption glycoprotein C (gC) heparan sulfate (HS) duck plague virus (DPV) |
Language | English |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-c460t-a63b9f17dcd29fb9d35c485496a812107e43e517e5ccba86b41512df6c9717083 |
Notes | 10-1039/S 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. ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
OpenAccessLink | https://doaj.org/article/a5e3df0afcfa4ef7bed756bf60eeba00 |
PQID | 2000473049 |
PQPubID | 24069 |
PageCount | 8 |
ParticipantIDs | doaj_primary_oai_doaj_org_article_a5e3df0afcfa4ef7bed756bf60eeba00 wanfang_journals_zgnykx_e201705019 proquest_miscellaneous_2000473049 crossref_primary_10_1016_S2095_3119_16_61550_2 crossref_citationtrail_10_1016_S2095_3119_16_61550_2 chongqing_primary_672072940 |
ProviderPackageCode | CITATION AAYXX |
PublicationCentury | 2000 |
PublicationDate | 2017-05-01 |
PublicationDateYYYYMMDD | 2017-05-01 |
PublicationDate_xml | – month: 05 year: 2017 text: 2017-05-01 day: 01 |
PublicationDecade | 2010 |
PublicationTitle | Journal of Integrative Agriculture |
PublicationTitleAlternate | Agricultural Sciences in China |
PublicationTitle_FL | Journal of Integrative Agriculture |
PublicationYear | 2017 |
Publisher | Key Laboratory of Animal Diseases and Human Health of Sichuan Province, Chengdu 611130, P.R.China 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 |
Publisher_xml | – name: Key Laboratory of Animal Diseases and Human Health of Sichuan Province, Chengdu 611130, P.R.China – name: 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 – name: KeAi Communications Co., Ltd |
References | Liman (10.1016/S2095-3119(16)61550-2_bib18) 2000; 145 Pavlova (10.1016/S2095-3119(16)61550-2_bib21) 2010; 91 Allen (10.1016/S2095-3119(16)61550-2_bib1) 1988; 62 Jogger (10.1016/S2095-3119(16)61550-2_bib12) 2004; 318 Walid (10.1016/S2095-3119(16)61550-2_bib35) 2010; 151 Wang (10.1016/S2095-3119(16)61550-2_bib36) 2011; 160 Sun (10.1016/S2095-3119(16)61550-2_bib30) 2014; 13 Chang (10.1016/S2095-3119(16)61550-2_bib6) 2010; 7 Tiwari (10.1016/S2095-3119(16)61550-2_bib32) 2004; 85 Klyachkin (10.1016/S2095-3119(16)61550-2_bib14) 2008; 374 Zou (10.1016/S2095-3119(16)61550-2_bib40) 2010; 7 Arumugam (10.1016/S2095-3119(16)61550-2_bib2) 2014; 72 Myung-Jin (10.1016/S2095-3119(16)61550-2_bib20) 2010; 391 Spear (10.1016/S2095-3119(16)61550-2_bib27) 2006; 344 Wu (10.1016/S2095-3119(16)61550-2_bib37) 2012; 86 Schmidtke (10.1016/S2095-3119(16)61550-2_bib26) 2003; 311 Yabe (10.1016/S2095-3119(16)61550-2_bib39) 2015; 472 Campagnolo (10.1016/S2095-3119(16)61550-2_bib5) 2001; 45 Sun (10.1016/S2095-3119(16)61550-2_bib31) 2013; 10 Rue (10.1016/S2095-3119(16)61550-2_bib22) 2003; 307 Spillmann (10.1016/S2095-3119(16)61550-2_bib28) 2001; 83 Gerber (10.1016/S2095-3119(16)61550-2_bib8) 1995; 214 Lee (10.1016/S2095-3119(16)61550-2_bib15) 2001; 63 Trybala (10.1016/S2095-3119(16)61550-2_bib33) 2000; 74 Marchetti (10.1016/S2095-3119(16)61550-2_bib19) 2004; 318 Trybala (10.1016/S2095-3119(16)61550-2_bib34) 2004; 62 Flamand (10.1016/S2095-3119(16)61550-2_bib7) 2001; 75 Lian (10.1016/S2095-3119(16)61550-2_bib17) 2010; 7 Wu (10.1016/S2095-3119(16)61550-2_bib38) 2012; 86 Atanasiu (10.1016/S2095-3119(16)61550-2_bib3) 2013; 4 Baldwin (10.1016/S2095-3119(16)61550-2_bib4) 2013; 7 Hu (10.1016/S2095-3119(16)61550-2_bib9) 2013; 174 Stanway (10.1016/S2095-3119(16)61550-2_bib29) 2005 Jacquet (10.1016/S2095-3119(16)61550-2_bib10) 1998; 53 Rux (10.1016/S2095-3119(16)61550-2_bib23) 2002; 294 Jarosinski (10.1016/S2095-3119(16)61550-2_bib11) 2012; 86 Kingsley (10.1016/S2095-3119(16)61550-2_bib13) 1999; 256 Lian (10.1016/S2095-3119(16)61550-2_bib16) 2011; 8 Saravanan (10.1016/S2095-3119(16)61550-2_bib24) 2014; 72 Sawitzky (10.1016/S2095-3119(16)61550-2_bib25) 1996; 41 |
References_xml | – volume: 294 start-page: 324 year: 2002 ident: 10.1016/S2095-3119(16)61550-2_bib23 article-title: Kinetic analysis of glycoprotein C of herpes simplex virus types 1 and 2 binding to heparin, heparan sulfate, and complement component C3b publication-title: Virology doi: 10.1006/viro.2001.1326 – volume: 53 start-page: 197 year: 1998 ident: 10.1016/S2095-3119(16)61550-2_bib10 article-title: The varicella zoster virus glycoprotein B (gB) plays a role in virus binding to cell surface heparan sulfate proteoglycans publication-title: Virus Research doi: 10.1016/S0168-1702(97)00149-4 – volume: 63 start-page: 427 year: 2001 ident: 10.1016/S2095-3119(16)61550-2_bib15 article-title: Heparin inhibits plaque formation by cell-free Marek's disease viruses in vitro publication-title: Journal of Veterinary Medical Science doi: 10.1292/jvms.63.427 – volume: 86 start-page: 13841 year: 2012 ident: 10.1016/S2095-3119(16)61550-2_bib38 article-title: Comparative genomic analysis of duck enteritis virus strains publication-title: Journal of Virology doi: 10.1128/JVI.01517-12 – volume: 174 start-page: 1 year: 2013 ident: 10.1016/S2095-3119(16)61550-2_bib9 article-title: Glycoprotein C plays a role in the adsorption of duck enteritis virus to chicken embryo fibroblasts cells and in infectivity publication-title: Virus Research doi: 10.1016/j.virusres.2013.01.015 – start-page: 757 year: 2005 ident: 10.1016/S2095-3119(16)61550-2_bib29 article-title: Virus taxonomy: Eighth report of the international committee on taxonomy of viruses – volume: 8 start-page: 1139 year: 2011 ident: 10.1016/S2095-3119(16)61550-2_bib16 article-title: Induction of immune responses in ducks with a DNA vaccine encoding duck plague virus glycoprotein C publication-title: Virology Journal doi: 10.1186/1743-422X-8-214 – volume: 86 start-page: 5965 year: 2012 ident: 10.1016/S2095-3119(16)61550-2_bib37 article-title: Complete genomic sequence of Chinese virulent duck enteritis virus publication-title: Journal of Virology doi: 10.1128/JVI.00529-12 – volume: 72 start-page: 45 year: 2014 ident: 10.1016/S2095-3119(16)61550-2_bib24 article-title: Isolation of low-molecular-weight heparin/heparan sulfate from marine sources publication-title: Advances in Food and Nutrition Research doi: 10.1016/B978-0-12-800269-8.00003-8 – volume: 311 start-page: 134 year: 2003 ident: 10.1016/S2095-3119(16)61550-2_bib26 article-title: Binding of a N,N'-bisheteryl derivative of dispirotripiperazine to heparan sulfate residues on the cell surface specifically prevents infection of viruses from different families publication-title: Virology doi: 10.1016/S0042-6822(03)00166-1 – volume: 74 start-page: 9106 year: 2000 ident: 10.1016/S2095-3119(16)61550-2_bib33 article-title: Herpes simplex virus types 1 and 2 differ in their interaction with heparan sulfate publication-title: Journal of Virology doi: 10.1128/JVI.74.19.9106-9114.2000 – volume: 4 start-page: e00046 year: 2013 ident: 10.1016/S2095-3119(16)61550-2_bib3 article-title: Regulation of herpes simplex virus gB-induced cell-cell fusion by mutant forms of gH/gL in the absence of gD and cellular receptors publication-title: mBio doi: 10.1128/mBio.00046-13 – volume: 62 start-page: 125 year: 2004 ident: 10.1016/S2095-3119(16)61550-2_bib34 article-title: Structural and functional features of the polycationic peptide required for inhibition of herpes simplex virus invasion of cells publication-title: Antiviral Research doi: 10.1016/j.antiviral.2003.12.007 – volume: 7 start-page: 37 year: 2010 ident: 10.1016/S2095-3119(16)61550-2_bib40 article-title: Detection of anatid herpesvirus 1 gC gene by TaqMan fluorescent quantitative real-time PCR with specific primers and probe publication-title: Virology Journal doi: 10.1186/1743-422X-7-37 – volume: 10 start-page: 89 year: 2013 ident: 10.1016/S2095-3119(16)61550-2_bib31 article-title: Distribution characteristics of DNA vaccine encoded with glycoprotein C from Anatid herpesvirus 1 with chitosan and liposome as deliver carrier in ducks publication-title: Virology Journal doi: 10.1186/1743-422X-10-89 – volume: 145 start-page: 2047 year: 2000 ident: 10.1016/S2095-3119(16)61550-2_bib18 article-title: Glycoprotein C of bovine herpesvirus 5 (BHV-5) confers a distinct heparin-binding phenotype to BHV-1 publication-title: Archive of Virology doi: 10.1007/s007050070039 – volume: 318 start-page: 405 year: 2004 ident: 10.1016/S2095-3119(16)61550-2_bib19 article-title: Inhibition of herpes simplex virus infection by lactoferrin is dependent on interference with the virus binding to glycosaminoglycans publication-title: Virology doi: 10.1016/j.virol.2003.09.029 – volume: 75 start-page: 11137 year: 2001 ident: 10.1016/S2095-3119(16)61550-2_bib7 article-title: The absence of glycoprotein gL, but not gC or gK, severely impairs pseudorabies virus neuroinvasiveness publication-title: Journal of Virology doi: 10.1128/JVI.75.22.11137-11145.2001 – volume: 256 start-page: 213 year: 1999 ident: 10.1016/S2095-3119(16)61550-2_bib13 article-title: Infectious laryngotracheitis virus, an alpha herpesvirus that does not interact with cell surface heparan sulfate publication-title: Virology doi: 10.1006/viro.1999.9609 – volume: 214 start-page: 29 year: 1995 ident: 10.1016/S2095-3119(16)61550-2_bib8 article-title: Differences in the role of glycoprotein C of HSV-1 and HSV-2 in viral binding may contribute to serotype differences in cell tropism publication-title: Virology doi: 10.1006/viro.1995.9957 – volume: 391 start-page: 176 year: 2010 ident: 10.1016/S2095-3119(16)61550-2_bib20 article-title: A role for heparan sulfate in viral surfing publication-title: Biochemical & Biophysical Research Communication doi: 10.1016/j.bbrc.2009.11.027 – volume: 318 start-page: 318 year: 2004 ident: 10.1016/S2095-3119(16)61550-2_bib12 article-title: Effects of linker-insertion mutations in herpes simplex virus 1 gD on glycoprotein-induced fusion with cells expressing HVEM or nectin-1 publication-title: Virology doi: 10.1016/j.virol.2003.10.004 – volume: 472 start-page: 1 year: 2015 ident: 10.1016/S2095-3119(16)61550-2_bib39 article-title: Development of a photoreactive probe-based system for detecting heparin publication-title: Analytical Biochemistry doi: 10.1016/j.ab.2014.11.007 – volume: 85 start-page: 805 year: 2004 ident: 10.1016/S2095-3119(16)61550-2_bib32 article-title: A role for 3-O-sulfated heparan sulfate in cell fusion induced by herpes simplex virus type 1 publication-title: Journal of General Virology doi: 10.1099/vir.0.19641-0 – volume: 160 start-page: 316 year: 2011 ident: 10.1016/S2095-3119(16)61550-2_bib36 article-title: Complete genome sequence of virulent duck enteritis virus (DEV) strain 2085 and comparison with genome sequences of virulent and attenuated DEV strains publication-title: Virus Research doi: 10.1016/j.virusres.2011.07.004 – volume: 45 start-page: 522 year: 2001 ident: 10.1016/S2095-3119(16)61550-2_bib5 article-title: An outbreak of duck viral enteritis (duck plague) in domestic Muscovy ducks (Cairina moschata domesticus) in Illinois publication-title: Avian Diseases doi: 10.2307/1592999 – volume: 83 start-page: 811 year: 2001 ident: 10.1016/S2095-3119(16)61550-2_bib28 article-title: Heparan sulfate: anchor for viral intruders? publication-title: Biochimie doi: 10.1016/S0300-9084(01)01290-1 – volume: 374 start-page: 23 year: 2008 ident: 10.1016/S2095-3119(16)61550-2_bib14 article-title: Mutagenic analysis of herpes simplex virus type 1 glycoprotein L reveals the importance of an arginine-rich region for function publication-title: Virology doi: 10.1016/j.virol.2007.11.014 – volume: 7 start-page: 5 year: 2013 ident: 10.1016/S2095-3119(16)61550-2_bib4 article-title: Members of 3-O-sulfotransferases (3-OST) family: A valuable tool from zebrafish to humans for understanding herpes simplex virus entry publication-title: The Open Virology Journal doi: 10.2174/1874357901307010005 – volume: 13 start-page: 4505 year: 2014 ident: 10.1016/S2095-3119(16)61550-2_bib30 article-title: Bioinformatic analysis and characteristics of glycoprotein C encoded by the newly identified UL44 gene of duck plague virus publication-title: Genetics & Molecular Research doi: 10.4238/2014.June.17.2 – volume: 91 start-page: 847 year: 2010 ident: 10.1016/S2095-3119(16)61550-2_bib21 article-title: In vitro and in vivo characterization of glycoprotein C-deleted infectious laryngotracheitis virus publication-title: Journal of General Virology doi: 10.1099/vir.0.016634-0 – volume: 72 start-page: 125 year: 2014 ident: 10.1016/S2095-3119(16)61550-2_bib2 article-title: Biological activities of heparan sulfate publication-title: Advances in Food and Nutrition Research doi: 10.1016/B978-0-12-800269-8.00008-7 – volume: 307 start-page: 12 year: 2003 ident: 10.1016/S2095-3119(16)61550-2_bib22 article-title: A role for glycoprotein C in pseudorabies virus entry that is independent of virus attachment to heparan sulfate and which involves the actin cytoskeleton publication-title: Virology doi: 10.1016/S0042-6822(02)00024-7 – volume: 344 start-page: 17 year: 2006 ident: 10.1016/S2095-3119(16)61550-2_bib27 article-title: Different receptors binding to distinct interfaces on herpes simplex virus gD can trigger events leading to cell fusion and viral entry publication-title: Virology doi: 10.1016/j.virol.2005.09.016 – volume: 86 start-page: 7896 year: 2012 ident: 10.1016/S2095-3119(16)61550-2_bib11 article-title: Marek's disease virus expresses multiple UL44 (gC) variants through mRNA splicing that are all required for efficient horizontal transmission publication-title: Journal of Virology doi: 10.1128/JVI.00908-12 – volume: 7 start-page: 349 year: 2010 ident: 10.1016/S2095-3119(16)61550-2_bib17 article-title: Identification and characterization of duck plague virus glycoprotein C gene and gene product publication-title: Virology Journal doi: 10.1186/1743-422X-7-349 – volume: 7 start-page: 120 year: 2010 ident: 10.1016/S2095-3119(16)61550-2_bib6 article-title: Cloning, expression and characterization of gE protein of duck plague virus publication-title: Virology Journal doi: 10.1186/1743-422X-7-120 – volume: 41 start-page: 101 year: 1996 ident: 10.1016/S2095-3119(16)61550-2_bib25 article-title: Glycoprotein B (gB) of pseudorabies virus interacts specifically with the glycosaminoglycan heparin publication-title: Virus Research doi: 10.1016/0168-1702(95)01277-X – volume: 151 start-page: 1 year: 2010 ident: 10.1016/S2095-3119(16)61550-2_bib35 article-title: Glycoprotein C of equine herpesvirus 4 plays a role in viral binding to cell surface heparan sulfate publication-title: Virus Research doi: 10.1016/j.virusres.2010.03.003 – volume: 62 start-page: 2850 year: 1988 ident: 10.1016/S2095-3119(16)61550-2_bib1 article-title: Characterization of an equine herpesvirus type 1 gene encoding a glycoprotein (gp13) with homology to herpes simplex virus glycoprotein C publication-title: Journal of Virology doi: 10.1128/JVI.62.8.2850-2858.1988 |
SSID | ssj0001550068 |
Score | 2.1002548 |
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... |
SourceID | doaj wanfang proquest crossref chongqing |
SourceType | Open Website Aggregation Database Enrichment Source Index Database Publisher |
StartPage | 1145 |
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 |
URI | http://lib.cqvip.com/qk/86610A/201705/672072940.html https://www.proquest.com/docview/2000473049 https://d.wanfangdata.com.cn/periodical/zgnykx-e201705019 https://doaj.org/article/a5e3df0afcfa4ef7bed756bf60eeba00 |
Volume | 16 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV2_b9UwELagEhIMiJ8itFQGMcCQNslz7ITtUVFVSDAAlbpZjn1Oq0ZJm7yA2gHxp3OX5IXXqQtLpES2E9nnu--cu-8Ye0uU7LFScVjExoTCyCzMpI1CkSSAgALQYtGB_pev8uhYfD5JTzZKfVFM2EgPPE7cvklh4XxkvPVGgFcFOJXKwssIoDDR4K2jzdtwpsb84JSSH6iyHGIIVDRx_i99Z__7_PBdLN_Tn7koTIhc4bSpy0s0GTeM1MDlfwOA3vtlam_qcsMSHT5iDycIyZfjpz9md6B-wh4sy3ai0YCn7M-3pgLeeO56e84vKlP2wH-etX3Hy-rKNgM7w1nNDzheKMy34sZ1TTvojw98WXS04WkAysSkaCJOvBLtmAXRcTq95XTmz7u-9QabngKRiNd4X3mEr8_Y8eGnHwdH4VRrIbRCRqvQyEWR-1g565LcF7lbpFZk6DxKkxHHmAKxgDRWkFpbmEwWgqCC89Lm6BAijnvOtuqmhhcM3y6Ig0c6Aej7QWRQt-dSpE6BF8r5gG3PE60vRk4NLVVCHOYiCphYT722E005Vcuo9ByPRqunafU03g2rp5OA7c3d1mPe0uEjrevcmGi2hwcofHoSPn2b8AXs9VoqNG5LmndTQ9N3VN0zEor-YQbszSQuelIPnb4u66tzVEzJwGaEKPvl__iabXafBhzDMXfY1qrt4RVCplWxy-7u_Y53hz3yF8q7E8k |
linkProvider | Directory of Open Access Journals |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Role+of+duck+plague+virus+glycoprotein+C+in+viral+adsorption%3A+Absence+of+specific+interactions+with+cell+surface+heparan+sulfate&rft.jtitle=Journal+of+Integrative+Agriculture&rft.au=JING%2C+Yan-chun&rft.au=Wu%2C+Ying&rft.au=SUN%2C+Kun-feng&rft.au=Wang%2C+Mingshu&rft.date=2017-05-01&rft.issn=2095-3119&rft.volume=16&rft.issue=5+p.1145-1152&rft.spage=1145&rft.epage=1152&rft_id=info:doi/10.1016%2FS2095-3119%2816%2961550-2&rft.externalDBID=NO_FULL_TEXT |
thumbnail_s | http://utb.summon.serialssolutions.com/2.0.0/image/custom?url=http%3A%2F%2Fimage.cqvip.com%2Fvip1000%2Fqk%2F86610A%2F86610A.jpg http://utb.summon.serialssolutions.com/2.0.0/image/custom?url=http%3A%2F%2Fwww.wanfangdata.com.cn%2Fimages%2FPeriodicalImages%2Fzgnykx-e%2Fzgnykx-e.jpg |