Epitope determinants of a chimpanzee Fab antibody that efficiently cross-neutralizes dengue type 1 and type 2 viruses map to inside and in close proximity to fusion loop of the dengue type 2 virus envelope glycoprotein.
about
Possible future monoclonal antibody (mAb)-based therapy against arbovirus infectionsMonoclonal antibody-mediated enhancement of dengue virus infection in vitro and in vivo and strategies for preventionProtective and therapeutic capacity of human single-chain Fv-Fc fusion proteins against West Nile virusWest Nile virus in complex with the Fab fragment of a neutralizing monoclonal antibodyCryptic Properties of a Cluster of Dominant Flavivirus Cross-Reactive Antigenic SitesCrystal Structure of West Nile Virus Envelope Glycoprotein Reveals Viral Surface EpitopesAntibody Recognition and Neutralization Determinants on Domains I and II of West Nile Virus Envelope ProteinInduction of Epitope-Specific Neutralizing Antibodies against West Nile VirusEpitope Determinants of a Chimpanzee Dengue Virus Type 4 (DENV-4)-Neutralizing Antibody and Protection against DENV-4 Challenge in Mice and Rhesus Monkeys by Passively Transferred Humanized AntibodyType- and Subcomplex-Specific Neutralizing Antibodies against Domain III of Dengue Virus Type 2 Envelope Protein Recognize Adjacent EpitopesMonoclonal Antibodies That Bind to Common Epitopes on the Dengue Virus Type 2 Nonstructural-1 and Envelope Glycoproteins Display Weak Neutralizing Activity and Differentiated Responses to Virulent Strains: Implications for Pathogenesis and VaccinesHumanized Monoclonal Antibodies Derived from Chimpanzee Fabs Protect against Japanese Encephalitis Virus In Vitro and In VivoAntibodies to Envelope Glycoprotein of Dengue Virus during the Natural Course of Infection Are Predominantly Cross-Reactive and Recognize Epitopes Containing Highly Conserved Residues at the Fusion Loop of Domain IIClosing the door on flaviviruses: Entry as a target for antiviral drug designThe structural immunology of antibody protection against West Nile virusHumoral Immune Responses of Dengue Fever Patients Using Epitope-Specific Serotype-2 Virus-Like Particle AntigensStructural Insights into the Mechanisms of Antibody-Mediated Neutralization of Flavivirus Infection: Implications for Vaccine DevelopmentImpact of Quaternary Organization on the Antigenic Structure of the Tick-Borne Encephalitis Virus Envelope Glycoprotein EDengue virus neutralization is modulated by IgG antibody subclass and Fcγ receptor subtypeThe Development of Therapeutic Antibodies That Neutralize Homologous and Heterologous Genotypes of Dengue Virus Type 1Structure of the St. Louis Encephalitis Virus Postfusion Envelope TrimerIdentification of a New Broadly Cross-reactive Epitope within Domain III of the Duck Tembusu Virus E ProteinPathogenesis and Inhibition of Flaviviruses from a Carbohydrate PerspectiveChimpanzee Fab fragments and a derived humanized immunoglobulin G1 antibody that efficiently cross-neutralize dengue type 1 and type 2 viruses.A broadly flavivirus cross-neutralizing monoclonal antibody that recognizes a novel epitope within the fusion loop of E protein.Structure and function analysis of therapeutic monoclonal antibodies against dengue virus type 2.Epitope reactions can be gauged by relative antibody discriminating specificity (RADS) values supported by deletion, substitution and cysteine bridge formation analyses: potential uses in pathogenesis studies.Development of a humanized antibody with high therapeutic potential against dengue virus type 2Mechanistic study of broadly neutralizing human monoclonal antibodies against dengue virus that target the fusion loop.Variation of the specificity of the human antibody responses after tick-borne encephalitis virus infection and vaccination.Dissection of antibody specificities induced by yellow fever vaccinationA Highly Sensitive Diagnostic System for Detecting Dengue Viruses Using the Interaction between a Sulfated Sugar Chain and a Virion.Characterization of a Novel Dengue Serotype 4 Virus-Specific Neutralizing Epitope on the Envelope Protein Domain III.The molecular basis of antibody-mediated neutralization of West Nile virus.Fusion loop peptide of the West Nile virus envelope protein is essential for pathogenesis and is recognized by a therapeutic cross-reactive human monoclonal antibody.DENV-2 subunit proteins fused to CR2 receptor-binding domain (P28)-induces specific and neutralizing antibodies to the Dengue virus in mice.Receptors and routes of dengue virus entry into the host cells.Generation and characterization of a monoclonal antibody that cross-reacts with the envelope protein from the four dengue virus serotypes.Manipulation of immunodominant dengue virus E protein epitopes reduces potential antibody-dependent enhancement.Intrahost Selection Pressures Drive Rapid Dengue Virus Microevolution in Acute Human Infections.
P2860
Q24289014-FD677F68-C2B1-4382-ADF8-1F314410D8EEQ24684689-0273CA80-D5E4-474B-ADBE-2E96DB2669EFQ27472711-60B5D153-ABCC-4375-B227-F9F9319121C1Q27477479-D72FB43D-1209-4B08-AA96-E6DFEEB3ED33Q27477542-3034FD84-074D-4BFC-B241-6DA4F9D6C0E3Q27477610-B5D1FCEB-32A3-4350-8F8A-3C3AAAD06B21Q27477718-9FC45D7E-FB63-4982-9B0F-0C5C391E8B09Q27484980-A1394A80-2824-461B-AB6D-419BDC6FCD5AQ27485025-0466291F-FED8-44EA-9851-C6CBB738ACFDQ27485031-F0D63F08-9AF2-4F5D-8B69-82BDF198519CQ27485490-61179B9A-4126-4258-AE1E-2C8B026FE5F0Q27486404-20725D60-B2FD-481A-814B-4316945C89A6Q27486409-5CCD7530-ACFD-4911-A88D-C238A665EAA4Q27487953-B952C35D-BACD-4DFF-851B-BB067CAE1A10Q27487955-DB5894B5-1943-4079-BFD6-87151288AD20Q27488243-2DEE82DF-6975-49C2-93AA-F00045F5685CQ27488364-E848C935-E3B6-4FAB-A61D-DE0EEF012F40Q27489515-7FC829DA-3D03-48C3-9631-F4D7953843EFQ27490436-D4C1ECAB-1EC2-458E-8318-53233955FB36Q27491317-9CB7BD65-0AA8-4A6B-9B94-A8229F294A09Q27674868-9502A2F3-112F-4C26-8BA5-3115DC786E0CQ27927982-70476D9E-4301-4047-ABC7-1BA8C624D3F1Q29994529-E6082C50-EBAB-4F37-B761-5026254F77D5Q33208947-730F87B5-F977-4440-9D51-3B830977478FQ33802834-1865D5E1-702A-42AB-BC5D-8AC08D00B76BQ34120070-F3140926-9CB4-4EB5-8A68-8EB63F4F19F0Q34251847-7F901174-9191-44D6-8113-9FBE43AA7DEBQ34260219-BDEC95E8-B639-4ADF-8EF7-9CAF3EAABFDFQ34306877-C842D9B5-73F0-4DCB-9B79-0AF85E44B1F5Q34594111-F0D2509F-07BD-433A-8477-72F154853DC4Q34789343-B5EEEA9F-EED4-4725-B3CD-CEC0EC6D0639Q35641137-0DEDC32B-152B-4E81-B58F-12F852709349Q35796610-7F2D9BB8-BA59-4EC6-942D-67E83F1E5925Q36842733-F691A380-2B7A-4811-BE69-01C8D40EE89EQ36950014-C0BFC3D1-4C08-452E-B2A7-74DEC508AE34Q37694852-C7ABA9E8-0C5B-4875-A150-B5E2F59E2BB9Q38366005-A5514C49-D923-4E57-9C19-955BE7140AEBQ39208408-47D3BDC7-FC41-4B2A-A71C-83DD353E9C08Q39329367-FA4DE004-938B-489B-9F15-EE84B07B9AA4Q40038877-EB845DBE-838F-49BE-A657-0F3CC3731978
P2860
Epitope determinants of a chimpanzee Fab antibody that efficiently cross-neutralizes dengue type 1 and type 2 viruses map to inside and in close proximity to fusion loop of the dengue type 2 virus envelope glycoprotein.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on December 2004
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Epitope determinants of a chim ...... 2 virus envelope glycoprotein.
@en
Epitope determinants of a chim ...... 2 virus envelope glycoprotein.
@nl
type
label
Epitope determinants of a chim ...... 2 virus envelope glycoprotein.
@en
Epitope determinants of a chim ...... 2 virus envelope glycoprotein.
@nl
prefLabel
Epitope determinants of a chim ...... 2 virus envelope glycoprotein.
@en
Epitope determinants of a chim ...... 2 virus envelope glycoprotein.
@nl
P2093
P2860
P921
P1433
P1476
Epitope determinants of a chim ...... 2 virus envelope glycoprotein.
@en
P2093
Ana P Goncalvez
Ching-Juh Lai
Robert H Purcell
P2860
P304
12919-12928
P356
10.1128/JVI.78.23.12919-12928.2004
P407
P577
2004-12-01T00:00:00Z