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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.
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
ISSN: 19326203
DOI: 10.1371/journal.pone.0033451
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