Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0033451
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dc.titleA human PrM antibody that recognizes a novel cryptic epitope on dengue E glycoprotein
dc.contributor.authorChan, A.H.Y.
dc.contributor.authorTan, H.C.
dc.contributor.authorChow, A.Y.
dc.contributor.authorLim, A.P.C.
dc.contributor.authorLok, S.M.
dc.contributor.authorMoreland, N.J.
dc.contributor.authorVasudevan, S.G.
dc.contributor.authorMacAry, P.A.
dc.contributor.authorOoi, E.E.
dc.contributor.authorHanson, B.J.
dc.date.accessioned2014-11-26T08:26:11Z
dc.date.available2014-11-26T08:26:11Z
dc.date.issued2012-04-03
dc.identifier.citationChan, A.H.Y., Tan, H.C., Chow, A.Y., Lim, A.P.C., Lok, S.M., Moreland, N.J., Vasudevan, S.G., MacAry, P.A., Ooi, E.E., Hanson, B.J. (2012-04-03). A human PrM antibody that recognizes a novel cryptic epitope on dengue E glycoprotein. PLoS ONE 7 (4) : -. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0033451
dc.identifier.issn19326203
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/109890
dc.description.abstractDengue virus (DENV) is a major mosquito-borne pathogen infecting up to 100 million people each year; so far no effective treatment or vaccines are available. Recently, highly cross-reactive and infection-enhancing pre-membrane (prM)-specific antibodies were found to dominate the anti-DENV immune response in humans, raising concern over vaccine candidates that contain native dengue prM sequences. In this study, we have isolated a broadly cross-reactive prM-specific antibody, D29, during a screen with a non-immunized human Fab-phage library against the four serotypes of DENV. The antibody is capable of restoring the infectivity of virtually non-infectious immature DENV (imDENV) in FcγR-bearing K562 cells. Remarkably, D29 also cross-reacted with a cryptic epitope on the envelope (E) protein located to the DI/DII junction as evidenced by site-directed mutagenesis. This cryptic epitope, while inaccessible to antibody binding in a native virus particle, may become exposed if E is not properly folded. These findings suggest that generation of anti-prM antibodies that enhance DENV infection may not be completely avoided even with immunization strategies employing E protein alone or subunits of E proteins. © 2012 Chan et al.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1371/journal.pone.0033451
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentDUKE-NUS GRADUATE MEDICAL SCHOOL S'PORE
dc.description.doi10.1371/journal.pone.0033451
dc.description.sourcetitlePLoS ONE
dc.description.volume7
dc.description.issue4
dc.description.page-
dc.identifier.isiut000304805900007
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