Peptide Paratope Mimics of the Broadly Neutralizing HIV-1 Antibody b12
| Autor: | Christina Haußner, Anette Rohrhofer, Sandra Nirschl, Barbara Schmidt, Dominik Damm, Jutta Eichler |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Anti-HIV Agents Peptide HIV Envelope Protein gp120 Protein Engineering 010402 general chemistry 01 natural sciences Biochemistry Cell Line 03 medical and health sciences In vivo Immunochemistry polycyclic compounds Humans Binding site Molecular Biology chemistry.chemical_classification Binding Sites biology Organic Chemistry Antibodies Monoclonal virus diseases nutritional and metabolic diseases Envelope glycoprotein GP120 Antibodies Neutralizing Virology In vitro 0104 chemical sciences 030104 developmental biology chemistry HIV-1 biology.protein Molecular Medicine Paratope Antibody Immunoglobulin Heavy Chains Peptides |
| Zdroj: | ChemBioChem. 18:647-653 |
| ISSN: | 1439-4227 |
| DOI: | 10.1002/cbic.201600621 |
| Popis: | The broadly neutralizing HIV-1 antibody b12 recognizes the CD4 binding site of the HIV-1 envelope glycoprotein gp120 and efficiently neutralizes HIV-1 infections in vitro and in vivo. Based on the 3D structure of a b12⋅gp120 complex, we have designed an assembled peptide (b12-M) that presents the parts of the three heavy-chain complementarity-determining regions (CDRs) of b12, which contain the contact sites of the antibody for gp120. This b12-mimetic peptide, as well as a truncated peptide presenting only two of the three heavy-chain CDRs of b12, were shown to recognize gp120 in a similar manner to b12, as well as to inhibit HIV-1 infection, demonstrating functional mimicry of b12 by the paratope mimetic peptides. |
| Databáze: | OpenAIRE |
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