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-Structure paper
タイトル | HIV envelope trimer-elicited autologous neutralizing antibodies bind a region overlapping the N332 glycan supersite. |
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ジャーナル・号・ページ | Sci Adv, Vol. 6, Issue 23, Page eaba0512, Year 2020 |
掲載日 | 2020年6月5日 |
著者 | Bartek Nogal / Laura E McCoy / Marit J van Gils / Christopher A Cottrell / James E Voss / Raiees Andrabi / Matthias Pauthner / Chi-Hui Liang / Terrence Messmer / Rebecca Nedellec / Mia Shin / Hannah L Turner / Gabriel Ozorowski / Rogier W Sanders / Dennis R Burton / Andrew B Ward / |
PubMed 要旨 | To date, immunization studies of rabbits with the BG505 SOSIP.664 HIV envelope glycoprotein trimers have revealed the 241/289 glycan hole as the dominant neutralizing antibody epitope. Here, we ...To date, immunization studies of rabbits with the BG505 SOSIP.664 HIV envelope glycoprotein trimers have revealed the 241/289 glycan hole as the dominant neutralizing antibody epitope. Here, we isolated monoclonal antibodies from a rabbit that did not exhibit glycan hole-dependent autologous serum neutralization. The antibodies did not compete with a previously isolated glycan hole-specific antibody but did compete with N332 glycan supersite broadly neutralizing antibodies. A 3.5-Å cryoEM structure of one of the antibodies in complex with the BG505 SOSIP.v5.2 trimer demonstrated that while the epitope recognized overlapped the N332 glycan supersite by contacting the GDIR motif at the base of V3, primary contacts were located in the variable V1 loop. These data suggest that strain-specific responses to V1 may interfere with broadly neutralizing responses to the N332 glycan supersite and vaccine immunogens may require engineering to minimize these off-target responses or steer them toward a more desirable pathway. |
リンク | Sci Adv / PubMed:32548265 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.52 - 25.0 Å |
構造データ | EMDB-21256, PDB-6vo0: EMDB-21498: EMDB-21499: EMDB-21500: |
化合物 | ChemComp-NAG: |
由来 |
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キーワード | VIRAL PROTEIN (ウイルスタンパク質) / HIV (ヒト免疫不全ウイルス) / Env / antibody (抗体) |