{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,12]],"date-time":"2026-09-12T06:04:07Z","timestamp":1789193047778,"version":"build-2803163510"},"reference-count":46,"publisher":"Public Library of Science (PLoS)","issue":"2","license":[{"start":{"date-parts":[[2013,2,6]],"date-time":"2013-02-06T00:00:00Z","timestamp":1360108800000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plosone.org"],"crossmark-restriction":false},"short-container-title":["PLoS ONE"],"DOI":"10.1371\/journal.pone.0054761","type":"journal-article","created":{"date-parts":[[2013,2,6]],"date-time":"2013-02-06T22:17:15Z","timestamp":1360189035000},"page":"e54761","update-policy":"https:\/\/doi.org\/10.1371\/journal.pone.corrections_policy","source":"Crossref","is-referenced-by-count":8,"title":["Interaction Domain of Glycoproteins gB and gH of Marek's Disease Virus and Identification of an Antiviral Peptide with Dual Functions"],"prefix":"10.1371","volume":"8","author":[{"given":"Xiao-Jing","family":"Chi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yi-Xin","family":"Lu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peng","family":"Zhao","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chuan-Gen","family":"Li","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiao-Jia","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ming","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2013,2,6]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1073\/pnas.82.3.751","article-title":"The structure of Marek disease virus DNA: the presence of unique expansion in nonpathogenic viral DNA","volume":"82","author":"K Fukuchi","year":"1985","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"7980","DOI":"10.1128\/JVI.74.17.7980-7988.2000","article-title":"The genome of a very virulent Marek's disease virus","volume":"74","author":"ER Tulman","year":"2000","journal-title":"J Virol"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"13879","DOI":"10.1073\/pnas.0305789101","article-title":"Marek's disease is a natural model for lymphomas overexpressing Hodgkin's disease antigen (CD30)","volume":"101","author":"SC Burgess","year":"2004","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"283","DOI":"10.1038\/nrmicro1382","article-title":"Marek's disease virus: from miasma to model","volume":"4","author":"N Osterrieder","year":"2006","journal-title":"Nat Rev Microbiol"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1354\/vp.38-5-491","article-title":"Marek's disease virus infection in the brain: virus replication, cellular infiltration, and major histocompatibility complex antigen expression","volume":"38","author":"IM Gimeno","year":"2001","journal-title":"Vet Pathol"},{"key":"ref6","first-page":"942","article-title":"Evaluation the immuno-protective effect of an infectious clone of meq- deleted Marek's disease virus","volume":"50","author":"Y Li","year":"2010","journal-title":"Wei Sheng Wu Xue Bao"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1637\/9048-090409-Reg.1","article-title":"A MEQ-deleted Marek's disease virus cloned as a bacterial artificial chromosome is a highly efficacious vaccine","volume":"54","author":"RF Silva","year":"2010","journal-title":"Avian Dis"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.virusres.2009.01.008","article-title":"In vitro characterization of the Meq proteins of Marek's disease virus vaccine strain CVI988","volume":"142","author":"DK Ajithdoss","year":"2009","journal-title":"Virus Res"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"690","DOI":"10.1038\/nsmb.1456","article-title":"Viral membrane fusion","volume":"15","author":"SC Harrison","year":"2008","journal-title":"Nat Struct Mol Biol"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"e32186","DOI":"10.1371\/journal.pone.0032186","article-title":"Biophysical characterization and membrane interaction of the two fusion loops of glycoprotein B from herpes simplex type I virus","volume":"7","author":"A Falanga","year":"2012","journal-title":"PLoS One"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1038\/nrmicro2548","article-title":"Fusing structure and function: a structural view of the herpesvirus entry machinery","volume":"9","author":"SA Connolly","year":"2011","journal-title":"Nat Rev Microbiol"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"1653","DOI":"10.1007\/s00018-008-7570-z","article-title":"Entry of herpesviruses into mammalian cells","volume":"65","author":"EE Heldwein","year":"2008","journal-title":"Cell Mol Life Sci"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"2017","DOI":"10.1099\/0022-1317-81-8-2017","article-title":"Characterization of cell-cell fusion mediated by herpes simplex virus 2 glycoproteins gB, gD, gH and gL in transfected cells","volume":"81","author":"MI Muggeridge","year":"2000","journal-title":"J Gen Virol"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"10559","DOI":"10.1073\/pnas.0801674105","article-title":"Native 3D intermediates of membrane fusion in herpes simplex virus 1 entry","volume":"105","author":"UE Maurer","year":"2008","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"12292","DOI":"10.1128\/JVI.01700-10","article-title":"Cascade of events governing cell-cell fusion induced by herpes simplex virus glycoproteins gD, gH\/gL, and gB","volume":"84","author":"D Atanasiu","year":"2010","journal-title":"J Virol"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"10187","DOI":"10.1073\/pnas.0703790104","article-title":"Herpes simplex virus glycoproteins gB and gH function in fusion between the virion envelope and the outer nuclear membrane","volume":"104","author":"A Farnsworth","year":"2007","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"9483","DOI":"10.1128\/JVI.75.19.9483-9492.2001","article-title":"Varicella-zoster Virus gB and gE coexpression, but not gB or gE alone, leads to abundant fusion and syncytium formation equivalent to those from gH and gL coexpression","volume":"75","author":"L Maresova","year":"2001","journal-title":"J Virol"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"18718","DOI":"10.1073\/pnas.0707452104","article-title":"Bimolecular complementation reveals that glycoproteins gB and gH\/gL of herpes simplex virus interact with each other during cell fusion","volume":"104","author":"D Atanasiu","year":"2007","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"11532","DOI":"10.1128\/JVI.01343-07","article-title":"Complexes between herpes simplex virus glycoproteins gD, gB, and gH detected in cells by complementation of split enhanced green fluorescent protein","volume":"81","author":"E Avitabile","year":"2007","journal-title":"J Virol"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1126\/science.1126548","article-title":"Crystal structure of glycoprotein B from herpes simplex virus 1","volume":"313","author":"EE Heldwein","year":"2006","journal-title":"Science"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1016\/0378-1119(94)90442-1","article-title":"Mutational analysis of the proteolytic cleavage site of glycoprotein B (gB) of Marek's disease virus","volume":"150","author":"S Yoshida","year":"1994","journal-title":"Gene"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"882","DOI":"10.1038\/nsmb.1837","article-title":"Crystal structure of the conserved herpesvirus fusion regulator complex gH-gL","volume":"17","author":"TK Chowdary","year":"2010","journal-title":"Nat Struct Mol Biol"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"760","DOI":"10.2174\/092986609788681850","article-title":"The role of glycoprotein H in herpesvirus membrane fusion","volume":"16","author":"HM Browne","year":"2009","journal-title":"Protein Pept Lett"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"4390","DOI":"10.1128\/JVI.76.9.4390-4400.2002","article-title":"Human herpesvirus 8 glycoprotein B (gB), gH, and gL can mediate cell fusion","volume":"76","author":"PE Pertel","year":"2002","journal-title":"J Vriol"},{"key":"ref25","first-page":"1085","article-title":"Analysis of synthetic peptides from heptad-repeat domains of herpes simplex virus type 1 glycoproteins H and B. J Gen Virol","volume":"87","author":"S Galdiero","year":"2006"},{"key":"ref26","first-page":"28632","article-title":"Fusogenic domains in herpes simplex virus type 1 glycoprotein H. J Biol Chem","volume":"280","author":"S Galdiero","year":"2005"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1002\/cbic.200700457","article-title":"The identification and characterization of fusogenic domains in herpes virus glycoprotein B molecules","volume":"9","author":"S Galdiero","year":"2008","journal-title":"Chembiochem"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"1461","DOI":"10.1016\/j.peptides.2008.04.022","article-title":"Peptides containing membrane-interacting motifs inhibit herpes simplex virus type 1 infectivity","volume":"29","author":"S Galdiero","year":"2008","journal-title":"Peptides"},{"key":"ref29","first-page":"190","article-title":"Structural characteristics and antiviral activity of multiple peptides derived from MDV glycoproteins B and H. Virol J","volume":"8","author":"X Wang","year":"2011"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"65","DOI":"10.1016\/j.virol.2011.05.001","article-title":"Characterisation and evaluation of antiviral recombinant peptides based on the heptad repeat regions of NDV and IBV fusion glycoproteins","volume":"416","author":"XJ Wang","year":"2011","journal-title":"Virology"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/j.sbi.2009.02.012","article-title":"Class III viral membrane fusion proteins","volume":"19","author":"M Backovic","year":"2009","journal-title":"Curr Opin Struct Biol"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"309","DOI":"10.1038\/nrm1076","article-title":"The structural biology of type I viral membrane fusion","volume":"4","author":"PM Colman","year":"2003","journal-title":"Nat Rev Mol Cell Biol"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"8333","DOI":"10.1128\/JVI.78.15.8333-8341.2004","article-title":"Coiled-coil domains in glycoproteins B and H are involved in human cytomegalovirus membrane fusion","volume":"78","author":"M Lopper","year":"2004","journal-title":"J Virol"},{"key":"ref34","first-page":"152","article-title":"Identification and characterization of glycoprotein H of MDV-1 GA strain","volume":"43","author":"P Wu","year":"1999","journal-title":"Acta Virol"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1292\/jvms.63.427","article-title":"Heparin inhibits plaque formation by cell-free Marek's disease viruses in vitro","volume":"63","author":"SI Lee","year":"2001","journal-title":"J Vet Med Sci"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"3716","DOI":"10.2174\/138161210794079218","article-title":"Inhibition of HIV-1 by fusion inhibitors","volume":"16","author":"D Eggink","year":"2010","journal-title":"Curr Pharm Des"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"11259","DOI":"10.1074\/jbc.M411141200","article-title":"Different from the HIV fusion inhibitor C34, the anti-HIV drug Fuzeon (T-20) inhibits HIV-1 entry by targeting multiple sites in gp41 and gp120","volume":"280","author":"S Liu","year":"2005","journal-title":"J Biol Chem"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"751","DOI":"10.2174\/092986609788681760","article-title":"Membrane fusion and fission: enveloped viruses","volume":"16","author":"A Falanga","year":"2009","journal-title":"Protein Pept Lett"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1146\/annurev.biochem.72.121801.161504","article-title":"Protein-lipid interplay in fusion and fission of biological membranes","volume":"72","author":"LV Chernomordik","year":"2003","journal-title":"Annu Rev Biochem"},{"key":"ref40","first-page":"2903","article-title":"Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B. Proc Natl Acad Sci U S A","volume":"104","author":"RP Subramanian","year":"2007"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"885","DOI":"10.1002\/cbic.200700044","article-title":"Evidence for a role of the membrane-proximal region of herpes simplex virus Type 1 glycoprotein H in membrane fusion and virus inhibition","volume":"8","author":"S Galdiero","year":"2007","journal-title":"Chembiochem"},{"key":"ref42","first-page":"29993","article-title":"Analysis of a membrane interacting region of herpes simplex virus type 1 glycoprotein H. J Biol Chem","volume":"283","author":"S Galdiero","year":"2008"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"2216","DOI":"10.1128\/JVI.80.5.2216-2224.2006","article-title":"Heptad repeat 2 in herpes simplex virus 1 gH interacts with heptad repeat 1 and is critical for virus entry and fusion","volume":"80","author":"T Gianni","year":"2006","journal-title":"J Virol"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"8190","DOI":"10.1128\/JVI.00504-06","article-title":"Hydrophobic alpha-helices 1 and 2 of herpes simplex virus gH interact with lipids, and their mimetic peptides enhance virus infection and fusion","volume":"80","author":"T Gianni","year":"2006","journal-title":"J Virol"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"1161","DOI":"10.1292\/jvms.61.1161","article-title":"Identification of the Marek's disease virus serotype 2 genes homologous to the glycoprotein B (UL27), ICP18.5 (UL28) and major DNA-binding protein (UL29) genes of herpes simplex virus type 1","volume":"61","author":"K Kato","year":"1999","journal-title":"J Vet Med Sci"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1002\/jss.400060102","article-title":"Cell shape and hexose transport in normal and virus-transformed cells in culture","volume":"6","author":"MJ Bissell","year":"1977","journal-title":"J Supramol Struct"}],"container-title":["PLoS ONE"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.pone.0054761","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2018,10,20]],"date-time":"2018-10-20T05:17:43Z","timestamp":1540012663000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.pone.0054761"}},"subtitle":[],"editor":[{"given":"Eric","family":"Cascales","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2013,2,6]]},"references-count":46,"journal-issue":{"issue":"2","published-online":{"date-parts":[[2013,2,6]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.pone.0054761","relation":{},"ISSN":["1932-6203"],"issn-type":[{"value":"1932-6203","type":"electronic"}],"subject":[],"published":{"date-parts":[[2013,2,6]]}}}