Please use this identifier to cite or link to this item: https://doi.org/10.1016/s0042-6822(03)00261-7
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dc.titleCharacterization of a 105-kDa plasma membrane associated glycoprotein that is involved in West Nile virus binding and infection
dc.contributor.authorChu, JJH
dc.contributor.authorNg, ML
dc.date.accessioned2020-08-25T02:46:12Z
dc.date.available2020-08-25T02:46:12Z
dc.date.issued2003-08-01
dc.identifier.citationChu, JJH, Ng, ML (2003-08-01). Characterization of a 105-kDa plasma membrane associated glycoprotein that is involved in West Nile virus binding and infection. Virology 312 (2) : 458-469. ScholarBank@NUS Repository. https://doi.org/10.1016/s0042-6822(03)00261-7
dc.identifier.issn00426822
dc.identifier.issn10960341
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/173460
dc.description.abstractThis study attempts to isolate and characterize West Nile virus-binding molecules on the plasma membrane of Vero and murine neuroblastoma cells that is responsible for virus entry. Pretreatment of Vero cells with proteases, glycosidases (endoglycosidase H, α-mannosidase), and sodium periodate strongly inhibited West Nile virus infection, whereas treatments with phospholipases and heparinases had no effect. The virus overlay protein blot detected a 105-kDa molecule on the plasma membrane extract of Vero and murine neuroblastoma cells that bind to WN virus. Treatment of the 105-kDa molecules with β-mercaptoethanol resulted in the virus binding to a series of lower molecular weight bands ranging from 30 to 40 kDa. The disruption of disulfide-linked subunits did not affect virus binding. N-linked sugars with mannose residues on the 105-kDa membrane proteins were found to be important in virus binding. Specific antibodies against the 105-kDa glycoprotein were highly effective in blocking virus entry. These results strongly supported the possibility that the 105-kDa protease-sensitive glycoprotein with complex N-linked sugars could be the putative receptor for WN virus. © 2003 Elsevier Science (USA). All rights reserved.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/S0042-6822(03)00261-7
dc.publisherElsevier BV
dc.sourceElements
dc.subjectAnimals
dc.subjectCell Membrane
dc.subjectChlorocebus aethiops
dc.subjectGlycoproteins
dc.subjectMice
dc.subjectMolecular Weight
dc.subjectNeuroblastoma
dc.subjectProtein Binding
dc.subjectProtein Transport
dc.subjectReceptors, Virus
dc.subjectVero Cells
dc.subjectWest Nile virus
dc.typeArticle
dc.date.updated2020-06-23T10:47:52Z
dc.contributor.departmentDEPT OF MICROBIOLOGY & IMMUNOLOGY
dc.description.doi10.1016/s0042-6822(03)00261-7
dc.description.sourcetitleVirology
dc.description.volume312
dc.description.issue2
dc.description.page458-469
dc.description.codenVIRLA
dc.identifier.isiut000184948000020
dc.description.placeUnited States
dc.published.statePublished
dc.description.redepositcompleted
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