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Trimerization of the HIV Transmembrane Domain in Lipid Bilayers Modulates Broadly Neutralizing Antibody Binding

Title
Trimerization of the HIV Transmembrane Domain in Lipid Bilayers Modulates Broadly Neutralizing Antibody Binding
Authors
Reichart T.M.Baksh M.M.Rhee J.-K.Fiedler J.D.Sligar S.G.Finn M.G.Zwick M.B.Dawson P.E.
Ewha Authors
이진규
SCOPUS Author ID
이진규scopus
Issue Date
2016
Journal Title
Angewandte Chemie - International Edition
ISSN
1433-7851JCR Link
Keywords
AntibodiesHIVMembrane proteinsNanostructuresPeptides
Publisher
Wiley-VCH Verlag
Indexed
SCI; SCIE; SCOPUS scopus
Abstract
The membrane-proximal external region (MPER) of HIV gp41 is an established target of antibodies that neutralize a broad range of HIV isolates. To evaluate the role of the transmembrane (TM) domain, synthetic MPER-derived peptides were incorporated into lipid nanoparticles using natural and designed TM domains, and antibody affinity was measured using immobilized and solution-based techniques. Peptides incorporating the native HIV TM domain exhibit significantly stronger interactions with neutralizing antibodies than peptides with a monomeric TM domain. Furthermore, a peptide with a trimeric, three-helix bundle TM domain recapitulates the binding profile of the native sequence. These studies suggest that neutralizing antibodies can bind the MPER when the TM domain is a three-helix bundle and this presentation could influence the binding of neutralizing antibodies to the virus. Lipid-bilayer presentation of viral antigens in Nanodiscs is a new platform for evaluating neutralizing antibodies. © 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
DOI
10.1002/anie.201508421
Appears in Collections:
엘텍공과대학 > 식품공학전공 > Journal papers
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