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Trimerization of the HIV Transmembrane Domain in Lipid Bilayers Modulates Broadly Neutralizing Antibody Binding
- Trimerization of the HIV Transmembrane Domain in Lipid Bilayers Modulates Broadly Neutralizing Antibody Binding
- Reichart, Timothy M.; Baksh, Michael M.; Rhee, Jin-Kytt; Fiedler, Jason D.; Sligar, Stephen. G.; Finn, M. G.; Zwick, Michael B.; Dawson, Philip E.
- Ewha Authors
- SCOPUS Author ID
- Issue Date
- Journal Title
- ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
- ANGEWANDTE CHEMIE-INTERNATIONAL EDITION vol. 55, no. 8, pp. 2688 - 2692
- antibodies; HIV; membrane proteins; nanostructures; peptides
- WILEY-V C H VERLAG GMBH
- SCI; SCIE; SCOPUS
- Document Type
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- 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.
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