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. 2022 Dec 16;9:1080964. doi: 10.3389/fmolb.2022.1080964

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Copyright © 2022 Fredericks, East, Shi, Liu, Maschietto, Ayala, Cioffi, Cohen, Fairbrother, Lefort, Nau, Levy, Wang, Batista, Lisi and Monaghan.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Binding of the full-length NAb C135 to the spike trimer in two conformations. (A) Using the full-length anti-PD1 IgG4 to represent the full-length C135, constant domains are in blue, heavy chain in green, and light chain in cyan. (B) Two orthogonal views of the closed spike trimer (from PDB: 6vxx coordinates). (C) Two orthogonal views of the fully open (open-1) spike trimer (using symmetrized PDB: 6vyb coordinates). (D) Binding of one NAb C135 to the closed spike trimer in two orthogonal views. (E) Binding of three NAb C135 to the closed spike trimer in two orthogonal views. (F) Binding of three NAb C135 to the open spike trimer.