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A new class of highly potent, broadly neutralizing antibodies isolated from viremic patients infected with dengue virus.

Identifieur interne : 003024 ( PubMed/Corpus ); précédent : 003023; suivant : 003025

A new class of highly potent, broadly neutralizing antibodies isolated from viremic patients infected with dengue virus.

Auteurs : Wanwisa Dejnirattisai ; Wiyada Wongwiwat ; Sunpetchuda Supasa ; Xiaokang Zhang ; Xinghong Dai ; Alexander Rouvinski ; Amonrat Jumnainsong ; Carolyn Edwards ; Nguyen Than Ha Quyen ; Thaneeya Duangchinda ; Jonathan M. Grimes ; Wen-Yang Tsai ; Chih-Yun Lai ; Wei-Kung Wang ; Prida Malasit ; Jeremy Farrar ; Cameron P. Simmons ; Z Hong Zhou ; Felix A. Rey ; Juthathip Mongkolsapaya ; Gavin R. Screaton

Source :

RBID : pubmed:25501631

English descriptors

Abstract

Dengue is a rapidly emerging, mosquito-borne viral infection, with an estimated 400 million infections occurring annually. To gain insight into dengue immunity, we characterized 145 human monoclonal antibodies (mAbs) and identified a previously unknown epitope, the envelope dimer epitope (EDE), that bridges two envelope protein subunits that make up the 90 repeating dimers on the mature virion. The mAbs to EDE were broadly reactive across the dengue serocomplex and fully neutralized virus produced in either insect cells or primary human cells, with 50% neutralization in the low picomolar range. Our results provide a path to a subunit vaccine against dengue virus and have implications for the design and monitoring of future vaccine trials in which the induction of antibody to the EDE should be prioritized.

DOI: 10.1038/ni.3058
PubMed: 25501631

Links to Exploration step

pubmed:25501631

Le document en format XML

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<div type="abstract" xml:lang="en">Dengue is a rapidly emerging, mosquito-borne viral infection, with an estimated 400 million infections occurring annually. To gain insight into dengue immunity, we characterized 145 human monoclonal antibodies (mAbs) and identified a previously unknown epitope, the envelope dimer epitope (EDE), that bridges two envelope protein subunits that make up the 90 repeating dimers on the mature virion. The mAbs to EDE were broadly reactive across the dengue serocomplex and fully neutralized virus produced in either insect cells or primary human cells, with 50% neutralization in the low picomolar range. Our results provide a path to a subunit vaccine against dengue virus and have implications for the design and monitoring of future vaccine trials in which the induction of antibody to the EDE should be prioritized.</div>
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