Structure of Fab 76 in complex with BG505 SOSIP.664.

作者：A.W. Myers, Monika Chandravanshi, Leanne S. Whitmore, Brendan F. Kohrn, Amina Negash, Dung N. Nguyen (6308711), Pooja Ralli-Jain, Kendra Cruickshank (24141799), Amit A. Upadhyay, Tysheena Charles, Christopher T. Edwards, Eric Hunter (117369), Rama R. Amara, Marek K. Korzeniowski, Ling Niu (4423711), Edwin Pozharski, William D. Tolbert, Steven E. Bosinger (8777792), Scott R. Kennedy, Marzena Pazgier, Cynthia A. Derdeyn · 发表于：Figshare · 年份：2026 · DOI：10.1371/journal.ppat.1014268.g007 · 研究领域：Chemistry、Biophysics、Stereochemistry、Biochemistry、Computational biology

(A) Structural comparison of the Fab 76-BG505 SOSIP.664 complex illustrates its distinct binding mode as compared to the Fab 1A8-BG505 SOSIP.664 complex. V H and V L are colored darker and lighter surfaces, respectively. (B) Zoomed view of the Fab 76 and gp120 interface. Epitope glycans are displayed in sticks and spheres. (C) Structural overlay of Fab 76 and 1A8 complexes showing their lack of overlap and the conformational change of loop V5 (black) which is accompanied by the change in position of the N462 glycan. (D) Comparative interaction networks of 1A8 and 76 Fab residues (outer circle) with gp120 (inner grey circle), mapped in a 4 Å cutoff criterion. Dashed blue lines represent hydrogen bonds. (E) Epitope footprints of Fabs are shown as colored surfaces on the BG505 SOSIP.664 with the CD4 binding loop highlighted in orange. Epitope-associated glycans are represented as colored spheres and other glycans as grey spheres. Epitope footprint edges are outlined in red and the contribution of the footprint by the heavy and light chains shown in darker and lighter shades, respectively.