{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,24]],"date-time":"2026-06-24T13:20:35Z","timestamp":1782307235510,"version":"3.54.5"},"reference-count":41,"publisher":"Oxford University Press (OUP)","issue":"11","license":[{"start":{"date-parts":[[2018,2,26]],"date-time":"2018-02-26T00:00:00Z","timestamp":1519603200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/academic.oup.com\/journals\/pages\/about_us\/legal\/notices"}],"funder":[{"name":"Promotion of Science (JSPS) KAKENHI","award":["15K07716"],"award-info":[{"award-number":["15K07716"]}]},{"DOI":"10.13039\/501100001700","name":"Ministry of Education, Culture, Sports, Science and Technology","doi-asserted-by":"publisher","award":["16H06429"],"award-info":[{"award-number":["16H06429"]}],"id":[{"id":"10.13039\/501100001700","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001700","name":"Ministry of Education, Culture, Sports, Science and Technology","doi-asserted-by":"publisher","award":["16H06431"],"award-info":[{"award-number":["16H06431"]}],"id":[{"id":"10.13039\/501100001700","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001700","name":"Ministry of Education, Culture, Sports, Science and Technology","doi-asserted-by":"publisher","award":["16K21723"],"award-info":[{"award-number":["16K21723"]}],"id":[{"id":"10.13039\/501100001700","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2018,5,5]]},"DOI":"10.1093\/infdis\/jiy081","type":"journal-article","created":{"date-parts":[[2018,2,23]],"date-time":"2018-02-23T12:07:37Z","timestamp":1519387657000},"page":"1740-1749","source":"Crossref","is-referenced-by-count":69,"title":["The Role of Heparan Sulfate Proteoglycans as an Attachment Factor for Rabies Virus Entry and Infection"],"prefix":"10.1093","volume":"217","author":[{"given":"Michihito","family":"Sasaki","sequence":"first","affiliation":[{"name":"Division of Molecular Pathobiology, Hokkaido University, Sapporo"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paulina D","family":"Anindita","sequence":"additional","affiliation":[{"name":"Division of Molecular Pathobiology, Hokkaido University, Sapporo"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Naoto","family":"Ito","sequence":"additional","affiliation":[{"name":"Laboratory of Zoonotic Diseases, Faculty of Applied Biological Sciences, Gifu University, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Makoto","family":"Sugiyama","sequence":"additional","affiliation":[{"name":"Laboratory of Zoonotic Diseases, Faculty of Applied Biological Sciences, Gifu University, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael","family":"Carr","sequence":"additional","affiliation":[{"name":"Global Institution for Collaborative Research and Education, Hokkaido University, Sapporo"},{"name":"National Virus Reference Laboratory, School of Medicine, University College Dublin, Ireland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hideo","family":"Fukuhara","sequence":"additional","affiliation":[{"name":"Laboratory of Biomolecular Science, Faculty of Pharmaceutical Science, Hokkaido University, Sapporo"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Toyoyuki","family":"Ose","sequence":"additional","affiliation":[{"name":"Laboratory of Biomolecular Science, Faculty of Pharmaceutical Science, Hokkaido University, Sapporo"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Katsumi","family":"Maenaka","sequence":"additional","affiliation":[{"name":"Laboratory of Biomolecular Science, Faculty of Pharmaceutical Science, Hokkaido University, Sapporo"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ayato","family":"Takada","sequence":"additional","affiliation":[{"name":"Division of Global Epidemiology, Research Center for Zoonosis Control, Hokkaido University, Sapporo"},{"name":"Global Institution for Collaborative Research and Education, Hokkaido University, Sapporo"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William W","family":"Hall","sequence":"additional","affiliation":[{"name":"Global Institution for Collaborative Research and Education, Hokkaido University, Sapporo"},{"name":"Center for Research in Infectious Diseases, University College Dublin, Ireland"},{"name":"Global Virus Network, Baltimore, Maryland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yasuko","family":"Orba","sequence":"additional","affiliation":[{"name":"Division of Molecular Pathobiology, Hokkaido University, Sapporo"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hirofumi","family":"Sawa","sequence":"additional","affiliation":[{"name":"Division of Molecular Pathobiology, Hokkaido University, Sapporo"},{"name":"Global Institution for Collaborative Research and Education, Hokkaido University, Sapporo"},{"name":"Global Virus Network, Baltimore, Maryland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2018,2,26]]},"reference":[{"key":"key\n\t\t\t\t20180504225616_CIT0001","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1038\/nrmicro2260","article-title":"The cell biology of rabies virus: using stealth to reach the brain","volume":"8","author":"Schnell","year":"2010","journal-title":"Nat Rev Microbiol"},{"key":"key\n\t\t\t\t20180504225616_CIT0002","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1016\/B978-0-12-396547-9.00002-X","article-title":"Rabies virus","volume-title":"Rabies","author":"Wunner","year":"2013","edition":"3rd ed"},{"key":"key\n\t\t\t\t20180504225616_CIT0003","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1126\/science.7053569","article-title":"Is the acetylcholine receptor a rabies virus receptor","volume":"215","author":"Lentz","year":"1982","journal-title":"Science"},{"key":"key\n\t\t\t\t20180504225616_CIT0004","doi-asserted-by":"crossref","first-page":"7181","DOI":"10.1128\/JVI.72.9.7181-7190.1998","article-title":"The neural cell adhesion molecule is a receptor for rabies virus","volume":"72","author":"Thoulouze","year":"1998","journal-title":"J Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0005","doi-asserted-by":"crossref","first-page":"7250","DOI":"10.1093\/emboj\/17.24.7250","article-title":"Low-affinity nerve-growth factor receptor (P75NTR) can serve as a receptor for rabies virus","volume":"17","author":"Tuffereau","year":"1998","journal-title":"EMBO J"},{"key":"key\n\t\t\t\t20180504225616_CIT0006","doi-asserted-by":"crossref","first-page":"75","DOI":"10.1007\/BF01309725","article-title":"Characterization of protein involvement in rabies virus binding to BHK-21 cells","volume":"140","author":"Broughan","year":"1995","journal-title":"Arch Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0007","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1099\/0022-1317-67-1-47","article-title":"Involvement of gangliosides in rabies virus infection","volume":"67(pt 1)","author":"Superti","year":"1986","journal-title":"J Gen Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0008","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1007\/BF01310002","article-title":"Role of phospholipids in rhabdovirus attachment to CER cells. Brief report","volume":"81","author":"Superti","year":"1984","journal-title":"Arch Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0009","doi-asserted-by":"crossref","first-page":"691","DOI":"10.1128\/JVI.50.3.691-697.1984","article-title":"Characterization of saturable binding sites for rabies virus","volume":"50","author":"Wunner","year":"1984","journal-title":"J Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0010","article-title":"Heparan sulfate proteoglycans","volume":"3:a004952","author":"Sarrazin","year":"2011","journal-title":"Cold Spring Harb Perspect Biol"},{"key":"key\n\t\t\t\t20180504225616_CIT0011","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1002\/med.1026","article-title":"Cell surface heparan sulfate and its roles in assisting viral infections","volume":"22","author":"Liu","year":"2002","journal-title":"Med Res Rev"},{"key":"key\n\t\t\t\t20180504225616_CIT0012","doi-asserted-by":"crossref","first-page":"7357","DOI":"10.1128\/JVI.72.9.7357-7366.1998","article-title":"Adaptation of Sindbis virus to BHK cells selects for use of heparan sulfate as an attachment receptor","volume":"72","author":"Klimstra","year":"1998","journal-title":"J Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0013","doi-asserted-by":"crossref","first-page":"7349","DOI":"10.1128\/JVI.72.9.7349-7356.1998","article-title":"Binding of Sindbis virus to cell surface heparan sulfate","volume":"72","author":"Byrnes","year":"1998","journal-title":"J Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0014","doi-asserted-by":"crossref","first-page":"16026","DOI":"10.1073\/pnas.1110617108","article-title":"Heparan sulfate binding by natural eastern equine encephalitis viruses promotes neurovirulence","volume":"108","author":"Gardner","year":"2011","journal-title":"Proc Natl Acad Sci U S A"},{"key":"key\n\t\t\t\t20180504225616_CIT0015","doi-asserted-by":"crossref","first-page":"13767","DOI":"10.1128\/JVI.01364-12","article-title":"Heparan sulfate facilitates Rift Valley fever virus entry into the cell","volume":"86","author":"de Boer","year":"2012","journal-title":"J Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0016","doi-asserted-by":"crossref","first-page":"3295","DOI":"10.1128\/JVI.01621-12","article-title":"Filoviruses utilize glycosaminoglycans for their attachment to target cells","volume":"87","author":"Salvador","year":"2013","journal-title":"J Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0017","doi-asserted-by":"crossref","first-page":"611","DOI":"10.1128\/JVI.02226-12","article-title":"Enterovirus 71 uses cell surface heparan sulfate glycosaminoglycan as an attachment receptor","volume":"87","author":"Tan","year":"2013","journal-title":"J Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0018","doi-asserted-by":"crossref","first-page":"2385","DOI":"10.1128\/JVI.03116-13","article-title":"A single-amino-acid polymorphism in Chikungunya virus E2 glycoprotein influences glycosaminoglycan utilization","volume":"88","author":"Silva","year":"2014","journal-title":"J Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0019","doi-asserted-by":"crossref","first-page":"1621","DOI":"10.1007\/s00705-015-2408-0","article-title":"Porcine epidemic diarrhea virus uses cell-surface heparan sulfate as an attachment factor","volume":"160","author":"Huan","year":"2015","journal-title":"Arch Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0020","doi-asserted-by":"crossref","first-page":"e02427","DOI":"10.1128\/mBio.02427-14","article-title":"Heparan sulfate-dependent enhancement of henipavirus infection","volume":"6","author":"Mathieu","year":"2015","journal-title":"MBio"},{"key":"key\n\t\t\t\t20180504225616_CIT0021","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.00503-17","article-title":"Heparan sulfate proteoglycan is an important attachment factor for cell entry of Akabane and Schmallenberg viruses","volume":"91","author":"Murakami","year":"2017","journal-title":"J Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0022","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.virusres.2016.02.002","article-title":"Generation of recombinant rabies viruses encoding NanoLuc luciferase for antiviral activity assays","volume":"215","author":"Anindita","year":"2016","journal-title":"Virus Res"},{"key":"key\n\t\t\t\t20180504225616_CIT0023","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1111\/j.1365-2443.2011.01491.x","article-title":"Equine major histocompatibility complex class I molecules act as entry receptors that bind to equine herpesvirus-1 glycoprotein D","volume":"16","author":"Sasaki","year":"2011","journal-title":"Genes Cells"},{"key":"key\n\t\t\t\t20180504225616_CIT0024","doi-asserted-by":"crossref","first-page":"14764","DOI":"10.1073\/pnas.94.26.14764","article-title":"A system for functional analysis of Ebola virus glycoprotein","volume":"94","author":"Takada","year":"1997","journal-title":"Proc Natl Acad Sci U S A"},{"key":"key\n\t\t\t\t20180504225616_CIT0025","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/0042-6822(92)90465-2","article-title":"Rabies virus glycoprotein is a trimer","volume":"187","author":"Gaudin","year":"1992","journal-title":"Virology"},{"key":"key\n\t\t\t\t20180504225616_CIT0026","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1016\/j.jmb.2004.09.079","article-title":"Foldon, the natural trimerization domain of T4 fibritin, dissociates into a monomeric A-state form containing a stable beta-hairpin: atomic details of trimer dissociation and local beta-hairpin stability from residual dipolar couplings","volume":"344","author":"Meier","year":"2004","journal-title":"J Mol Biol"},{"key":"key\n\t\t\t\t20180504225616_CIT0027","doi-asserted-by":"crossref","first-page":"94","DOI":"10.4049\/jimmunol.72.1.94","article-title":"Studies on chick-embryo-adapted-rabies virus. VI. Further changes in pathogenic properties following prolonged cultivation in the developing chick embryo","volume":"72","author":"Koprowski","year":"1954","journal-title":"J Immunol"},{"key":"key\n\t\t\t\t20180504225616_CIT0028","doi-asserted-by":"crossref","first-page":"11072","DOI":"10.1128\/JVI.77.20.11072-11081.2003","article-title":"Identification of a heparin-binding motif on adeno-associated virus type 2 capsids","volume":"77","author":"Kern","year":"2003","journal-title":"J Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0029","doi-asserted-by":"crossref","first-page":"15193","DOI":"10.1074\/jbc.M800066200","article-title":"The HIV-1 envelope glycoprotein gp120 features four heparan sulfate binding domains, including the co-receptor binding site","volume":"283","author":"Crublet","year":"2008","journal-title":"J Biol Chem"},{"key":"key\n\t\t\t\t20180504225616_CIT0030","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1016\/S0092-8674(00)80058-6","article-title":"A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry","volume":"99","author":"Shukla","year":"1999","journal-title":"Cell"},{"key":"key\n\t\t\t\t20180504225616_CIT0031","doi-asserted-by":"crossref","first-page":"6629","DOI":"10.1128\/JVI.01988-05","article-title":"N- and 6-O-sulfated heparan sulfates mediate internalization of coxsackievirus B3 variant PD into CHO-K1 cells","volume":"80","author":"Zautner","year":"2006","journal-title":"J Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0032","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1016\/j.virol.2011.11.030","article-title":"O-sulfate groups of heparin are critical for inhibition of ecotropic murine leukemia virus infection by heparin","volume":"424","author":"Seki","year":"2012","journal-title":"Virology"},{"key":"key\n\t\t\t\t20180504225616_CIT0033","doi-asserted-by":"crossref","first-page":"3846","DOI":"10.1128\/JVI.03647-14","article-title":"Characterization of hepatitis C virus interaction with heparan sulfate proteoglycans","volume":"89","author":"Xu","year":"2015","journal-title":"J Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0034","doi-asserted-by":"crossref","DOI":"10.1128\/JVI.00432-17","article-title":"Genome-wide screening uncovers the significance of N-sulfation of heparan sulfate as a host cell factor for Chikungunya virus infection","volume":"91","author":"Tanaka","year":"2017","journal-title":"J Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0035","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1099\/vir.0.047852-0","article-title":"Addition of a single N-glycan to street rabies virus glycoprotein enhances virus production","volume":"94","author":"Yamada","year":"2013","journal-title":"J Gen Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0036","doi-asserted-by":"crossref","first-page":"3563","DOI":"10.1128\/JVI.02494-06","article-title":"Heparan sulfate binding can contribute to the neurovirulence of neuroadapted and nonneuroadapted Sindbis viruses","volume":"81","author":"Ryman","year":"2007","journal-title":"J Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0037","doi-asserted-by":"crossref","first-page":"5627","DOI":"10.1128\/JVI.75.12.5627-5637.2001","article-title":"Adaptation of tick-borne encephalitis virus to BHK-21 cells results in the formation of multiple heparan sulfate binding sites in the envelope protein and attenuation in vivo","volume":"75","author":"Mandl","year":"2001","journal-title":"J Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0038","doi-asserted-by":"crossref","first-page":"5115","DOI":"10.1128\/JVI.71.7.5115-5123.1997","article-title":"Tissue culture adaptation of foot-and-mouth disease virus selects viruses that bind to heparin and are attenuated in cattle","volume":"71","author":"Sa-Carvalho","year":"1997","journal-title":"J Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0039","doi-asserted-by":"crossref","first-page":"4901","DOI":"10.1128\/JVI.76.10.4901-4911.2002","article-title":"Mechanism of virulence attenuation of glycosaminoglycan-binding variants of Japanese encephalitis virus and Murray Valley encephalitis virus","volume":"76","author":"Lee","year":"2002","journal-title":"J Virol"},{"key":"key\n\t\t\t\t20180504225616_CIT0040","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1006\/viro.2000.0546","article-title":"Mutations in the E2 glycoprotein of Venezuelan equine encephalitis virus confer heparan sulfate interaction, low morbidity, and rapid clearance from blood of mice","volume":"276","author":"Bernard","year":"2000","journal-title":"Virology"},{"key":"key\n\t\t\t\t20180504225616_CIT0041","doi-asserted-by":"crossref","first-page":"e2719","DOI":"10.1371\/journal.pntd.0002719","article-title":"Deliberate attenuation of Chikungunya virus by adaptation to heparan sulfate-dependent infectivity: a model for rational arboviral vaccine design","volume":"8","author":"Gardner","year":"2014","journal-title":"PLoS Negl Trop Dis"}],"container-title":["The Journal of Infectious Diseases"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/academic.oup.com\/jid\/article-pdf\/217\/11\/1740\/24789861\/jiy081.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,9,1]],"date-time":"2023-09-01T07:44:33Z","timestamp":1693554273000},"score":1,"resource":{"primary":{"URL":"https:\/\/academic.oup.com\/jid\/article\/217\/11\/1740\/4909726"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,2,26]]},"references-count":41,"journal-issue":{"issue":"11","published-online":{"date-parts":[[2018,2,26]]},"published-print":{"date-parts":[[2018,5,5]]}},"URL":"https:\/\/doi.org\/10.1093\/infdis\/jiy081","relation":{},"ISSN":["0022-1899","1537-6613"],"issn-type":[{"value":"0022-1899","type":"print"},{"value":"1537-6613","type":"electronic"}],"subject":[],"published-other":{"date-parts":[[2018,6,1]]},"published":{"date-parts":[[2018,2,26]]}}}