A two-step mechanism for the binding of the HIV-1 MPER epitope by the 10E8 antibody onto biosensor-supported lipid bilayers
© 2024 Federation of European Biochemical Societies..
HIV-1 antibodies targeting the carboxy-terminal area of the membrane-proximal external region (ctMPER) are close to exerting viral pan-neutralization. Here, we reconstituted the ctMPER epitope as the N-terminal extremity of the Env glycoprotein transmembrane domain helix and immobilized it onto biosensor-supported lipid bilayers. We assessed the binding mechanism of anti-MPER antibody 10E8 through Surface Plasmon Resonance, and found, through equilibrium and kinetic binding analyses as a function of bilayer thickness, peptide length, and paratope mutations, that 10E8 engages first with the epitope peptide (encounter), limited by ctMPER helix accessibility at the membrane surface, and then inserts into the lipid bilayer assisted by favorable Fab-membrane interactions (docking). This mechanistic information may help in devising new strategies to develop more efficient MPER-targeting vaccines.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2024 |
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| Erschienen: |
2024 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:598 |
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| Enthalten in: |
FEBS letters - 598(2024), 7 vom: 27. Apr., Seite 787-800 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
García-Porras, Miguel [VerfasserIn] |
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| Links: |
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| Themen: |
Antibodies, Neutralizing |
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| Anmerkungen: |
Date Completed 09.04.2024 Date Revised 09.04.2024 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1002/1873-3468.14814 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM36829322X |
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| 100 | 1 | |a García-Porras, Miguel |e verfasserin |4 aut | |
| 245 | 1 | 2 | |a A two-step mechanism for the binding of the HIV-1 MPER epitope by the 10E8 antibody onto biosensor-supported lipid bilayers |
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| 500 | |a Date Revised 09.04.2024 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a © 2024 Federation of European Biochemical Societies. | ||
| 520 | |a HIV-1 antibodies targeting the carboxy-terminal area of the membrane-proximal external region (ctMPER) are close to exerting viral pan-neutralization. Here, we reconstituted the ctMPER epitope as the N-terminal extremity of the Env glycoprotein transmembrane domain helix and immobilized it onto biosensor-supported lipid bilayers. We assessed the binding mechanism of anti-MPER antibody 10E8 through Surface Plasmon Resonance, and found, through equilibrium and kinetic binding analyses as a function of bilayer thickness, peptide length, and paratope mutations, that 10E8 engages first with the epitope peptide (encounter), limited by ctMPER helix accessibility at the membrane surface, and then inserts into the lipid bilayer assisted by favorable Fab-membrane interactions (docking). This mechanistic information may help in devising new strategies to develop more efficient MPER-targeting vaccines | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a HIV neutralization | |
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| 650 | 4 | |a bnAb 10E8 | |
| 650 | 4 | |a supported lipid bilayers | |
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| 650 | 7 | |a Peptides |2 NLM | |
| 650 | 7 | |a HIV Envelope Protein gp41 |2 NLM | |
| 700 | 1 | |a Torralba, Johana |e verfasserin |4 aut | |
| 700 | 1 | |a Insausti, Sara |e verfasserin |4 aut | |
| 700 | 1 | |a Valle, Javier |e verfasserin |4 aut | |
| 700 | 1 | |a Andreu, David |e verfasserin |4 aut | |
| 700 | 1 | |a Apellániz, Beatriz |e verfasserin |4 aut | |
| 700 | 1 | |a Nieva, José L |e verfasserin |4 aut | |
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