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https://doi.org/10.1371/journal.pone.0033451
Title: | A human PrM antibody that recognizes a novel cryptic epitope on dengue E glycoprotein | Authors: | Chan, 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. |
Issue Date: | 3-Apr-2012 | Citation: | Chan, 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 | Abstract: | Dengue 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. | Source Title: | PLoS ONE | URI: | http://scholarbank.nus.edu.sg/handle/10635/109890 | ISSN: | 19326203 | DOI: | 10.1371/journal.pone.0033451 |
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