A potent anti‐dengue human antibody preferentially recognizes the conformation of E protein monomers assembled on the virus surface. Issue 3 (14th January 2014)

• Record Type: Journal Article
• Authors: Fibriansah, Guntur; Tan, Joanne L; Smith, Scott A; de, Adamberage R; Ng, Thiam‐Seng; Kostyuchenko, Victor A; Ibarra, Kristie D; Wang, Jiaqi; Harris, Eva; de, Aravinda; Crowe, James E; Lok, Shee‐Mei
• Is Part Of: EMBO molecular medicine. Volume 6:Issue 3(2014:Mar.)
• Page Start: 358
• Page End: 371
• Publication Date: 2014-01-14
• Subjects: Molecular biology -- Periodicals; Medical genetics -- Periodicals; Pathology, Molecular -- Periodicals; 616.04205
• DOI: 10.1002/emmm.201303404
• Languages: English
• ISSNs: 1757-4676

Abstract

<abstract abstract-type="synopsis" xml:lang="en" id="emmm201303404-abs-0002"> <title>Synopsis</title> <p> <boxed-text content-type="graphic" id="emmm201303404-blkfxd-0001" position="anchor" orientation="portrait"> <graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg4st018hx" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /> </boxed-text> </p> <p>Vaccine development against Dengue disease is complicated by the virus serotype priming to secondary infections. Structure of a potent human antibody 1F4 complexed with DENV serotype 1 highlights the hinge angle of the viral protein as critical for vaccine design.</p> <p> <list id="emmm201303404-list-0001" list-type="bullet"> <list-item> <p>DI‐DII hinge is a common epitope recognised by highly neutralising human antibodies.</p> </list-item> <list-item> <p>The conformation angle of the hinge is critical for 1F4 binding.</p> </list-item> <list-item> <p>1F4 recognises E protein monomers on the virus surface but not recombinant E proteins due to the conserved hinge angle of endogenous viral E proteins.</p> </list-item> </list> </p> </abstract>