A potent anti-dengue human antibody preferentially recognizes the conformation of E protein monomers assembled on the virus surface

10.1002/emmm.201303404

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Main Authors:	Fibriansah G., Tan J.L., Smith S.A., de Alwis A.R., Ng T.-S., Kostyuchenko V.A., Ibarra K.D., Wang J., Harris E., de Silva A., Crowe J.E., Lok S.-M.
Other Authors:	DUKE-NUS MEDICAL SCHOOL
Format:	Article
Published:	2020
Subjects:	CD209 antigen epitope genomic RNA human monoclonal antibody human monoclonal antibody 1F4 immunoglobulin F(ab) fragment immunoglobulin G immunoglobulin G1 membrane protein neutralizing antibody unclassified drug virus envelope protein virus receptor amino acid sequence animal experiment animal model animal tissue article bone marrow cell cell strain U937 complementarity determining region conformation controlled study cryoelectron microscopy dengue Dengue virus Dengue virus 1 Dengue virus 2 Dengue virus 3 Dengue virus 4 enzyme linked immunosorbent assay gene dosage glycosylation heavy chain hinge region human hydrogen bond in vitro study in vivo study lethal dose light chain limit of detection mature virus mouse nonhuman priority journal protein assembly protein conformation protein quaternary structure protein secondary structure receptor binding sequence alignment serodiagnosis serotype sublethal dose Vero cell virus attachment virus entry virus load virus morphology virus neutralization Amino Acid Sequence Animals Antibodies, Monoclonal Antibodies, Neutralizing Antibodies, Viral Cell Line Dengue Dengue Virus Epitopes Humans Immunoglobulin Fab Fragments Mice Molecular Dynamics Simulation Molecular Sequence Data Protein Structure, Tertiary Viral Envelope Proteins Virus Internalization
Online Access:	https://scholarbank.nus.edu.sg/handle/10635/174171
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Institution:	National University of Singapore

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spelling	sg-nus-scholar.10635-1741712024-11-14T07:51:58Z A potent anti-dengue human antibody preferentially recognizes the conformation of E protein monomers assembled on the virus surface Fibriansah G. Tan J.L. Smith S.A. de Alwis A.R. Ng T.-S. Kostyuchenko V.A. Ibarra K.D. Wang J. Harris E. de Silva A. Crowe J.E. Lok S.-M. DUKE-NUS MEDICAL SCHOOL CD209 antigen epitope genomic RNA human monoclonal antibody human monoclonal antibody 1F4 immunoglobulin F(ab) fragment immunoglobulin G immunoglobulin G1 membrane protein neutralizing antibody unclassified drug virus envelope protein virus receptor amino acid sequence animal experiment animal model animal tissue article bone marrow cell cell strain U937 complementarity determining region conformation controlled study cryoelectron microscopy dengue Dengue virus Dengue virus 1 Dengue virus 2 Dengue virus 3 Dengue virus 4 enzyme linked immunosorbent assay gene dosage glycosylation heavy chain hinge region human hydrogen bond in vitro study in vivo study lethal dose light chain limit of detection mature virus mouse nonhuman priority journal protein assembly protein conformation protein quaternary structure protein secondary structure receptor binding sequence alignment serodiagnosis serotype sublethal dose Vero cell virus attachment virus entry virus load virus morphology virus neutralization Amino Acid Sequence Animals Antibodies, Monoclonal Antibodies, Neutralizing Antibodies, Viral Cell Line Dengue Dengue Virus Epitopes Humans Immunoglobulin Fab Fragments Mice Molecular Dynamics Simulation Molecular Sequence Data Protein Structure, Tertiary Viral Envelope Proteins Virus Internalization 10.1002/emmm.201303404 EMBO Molecular Medicine 6 3 358-371 2020-09-03T10:42:45Z 2020-09-03T10:42:45Z 2014 Article Fibriansah G., Tan J.L., Smith S.A., de Alwis A.R., Ng T.-S., Kostyuchenko V.A., Ibarra K.D., Wang J., Harris E., de Silva A., Crowe J.E., Lok S.-M. (2014). A potent anti-dengue human antibody preferentially recognizes the conformation of E protein monomers assembled on the virus surface. EMBO Molecular Medicine 6 (3) : 358-371. ScholarBank@NUS Repository. https://doi.org/10.1002/emmm.201303404 17574676 https://scholarbank.nus.edu.sg/handle/10635/174171 Unpaywall 20200831
institution	National University of Singapore
building	NUS Library
continent	Asia
country	Singapore Singapore
content_provider	NUS Library
collection	ScholarBank@NUS
topic	CD209 antigen epitope genomic RNA human monoclonal antibody human monoclonal antibody 1F4 immunoglobulin F(ab) fragment immunoglobulin G immunoglobulin G1 membrane protein neutralizing antibody unclassified drug virus envelope protein virus receptor amino acid sequence animal experiment animal model animal tissue article bone marrow cell cell strain U937 complementarity determining region conformation controlled study cryoelectron microscopy dengue Dengue virus Dengue virus 1 Dengue virus 2 Dengue virus 3 Dengue virus 4 enzyme linked immunosorbent assay gene dosage glycosylation heavy chain hinge region human hydrogen bond in vitro study in vivo study lethal dose light chain limit of detection mature virus mouse nonhuman priority journal protein assembly protein conformation protein quaternary structure protein secondary structure receptor binding sequence alignment serodiagnosis serotype sublethal dose Vero cell virus attachment virus entry virus load virus morphology virus neutralization Amino Acid Sequence Animals Antibodies, Monoclonal Antibodies, Neutralizing Antibodies, Viral Cell Line Dengue Dengue Virus Epitopes Humans Immunoglobulin Fab Fragments Mice Molecular Dynamics Simulation Molecular Sequence Data Protein Structure, Tertiary Viral Envelope Proteins Virus Internalization
spellingShingle	CD209 antigen epitope genomic RNA human monoclonal antibody human monoclonal antibody 1F4 immunoglobulin F(ab) fragment immunoglobulin G immunoglobulin G1 membrane protein neutralizing antibody unclassified drug virus envelope protein virus receptor amino acid sequence animal experiment animal model animal tissue article bone marrow cell cell strain U937 complementarity determining region conformation controlled study cryoelectron microscopy dengue Dengue virus Dengue virus 1 Dengue virus 2 Dengue virus 3 Dengue virus 4 enzyme linked immunosorbent assay gene dosage glycosylation heavy chain hinge region human hydrogen bond in vitro study in vivo study lethal dose light chain limit of detection mature virus mouse nonhuman priority journal protein assembly protein conformation protein quaternary structure protein secondary structure receptor binding sequence alignment serodiagnosis serotype sublethal dose Vero cell virus attachment virus entry virus load virus morphology virus neutralization Amino Acid Sequence Animals Antibodies, Monoclonal Antibodies, Neutralizing Antibodies, Viral Cell Line Dengue Dengue Virus Epitopes Humans Immunoglobulin Fab Fragments Mice Molecular Dynamics Simulation Molecular Sequence Data Protein Structure, Tertiary Viral Envelope Proteins Virus Internalization Fibriansah G. Tan J.L. Smith S.A. de Alwis A.R. Ng T.-S. Kostyuchenko V.A. Ibarra K.D. Wang J. Harris E. de Silva A. Crowe J.E. Lok S.-M. A potent anti-dengue human antibody preferentially recognizes the conformation of E protein monomers assembled on the virus surface
description	10.1002/emmm.201303404
author2	DUKE-NUS MEDICAL SCHOOL
author_facet	DUKE-NUS MEDICAL SCHOOL Fibriansah G. Tan J.L. Smith S.A. de Alwis A.R. Ng T.-S. Kostyuchenko V.A. Ibarra K.D. Wang J. Harris E. de Silva A. Crowe J.E. Lok S.-M.
format	Article
author	Fibriansah G. Tan J.L. Smith S.A. de Alwis A.R. Ng T.-S. Kostyuchenko V.A. Ibarra K.D. Wang J. Harris E. de Silva A. Crowe J.E. Lok S.-M.
author_sort	Fibriansah G.
title	A potent anti-dengue human antibody preferentially recognizes the conformation of E protein monomers assembled on the virus surface
title_short	A potent anti-dengue human antibody preferentially recognizes the conformation of E protein monomers assembled on the virus surface
title_full	A potent anti-dengue human antibody preferentially recognizes the conformation of E protein monomers assembled on the virus surface
title_fullStr	A potent anti-dengue human antibody preferentially recognizes the conformation of E protein monomers assembled on the virus surface
title_full_unstemmed	A potent anti-dengue human antibody preferentially recognizes the conformation of E protein monomers assembled on the virus surface
title_sort	potent anti-dengue human antibody preferentially recognizes the conformation of e protein monomers assembled on the virus surface
publishDate	2020
url	https://scholarbank.nus.edu.sg/handle/10635/174171
_version_	1821208033678589952

A potent anti-dengue human antibody preferentially recognizes the conformation of E protein monomers assembled on the virus surface

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