7PNM

Human coronavirus OC43 spike glycoprotein ectodomain in complex with the 46C12 antibody Fab fragment

7PNM の概要

• エントリーDOI: 10.2210/pdb7pnm/pdb
• EMDBエントリー: 13549
• 分子名称: Spike glycoprotein, 46C12 antibody light chain, 46C12 antibody heavy chain, ... (5 entities in total)
• 機能のキーワード: coronavirus, glycoprotein, antibody, spike, viral protein
• 由来する生物種: Human coronavirus OC43 (HCoV-OC43); 詳細
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 527666.08

構造登録者

Hurdiss, D.L. (登録日: 2021-09-07, 公開日: 2022-04-20, 最終更新日: 2024-10-23)

主引用文献

Wang, C.,Hesketh, E.L.,Shamorkina, T.M.,Li, W.,Franken, P.J.,Drabek, D.,van Haperen, R.,Townend, S.,van Kuppeveld, F.J.M.,Grosveld, F.,Ranson, N.A.,Snijder, J.,de Groot, R.J.,Hurdiss, D.L.,Bosch, B.J.
Antigenic structure of the human coronavirus OC43 spike reveals exposed and occluded neutralizing epitopes.
Nat Commun, 13:2921-2921, 2022

PubMed Abstract: Human coronavirus OC43 is a globally circulating common cold virus sustained by recurrent reinfections. How it persists in the population and defies existing herd immunity is unknown. Here we focus on viral glycoprotein S, the target for neutralizing antibodies, and provide an in-depth analysis of its antigenic structure. Neutralizing antibodies are directed to the sialoglycan-receptor binding site in S1 domain, but, remarkably, also to S1. The latter block infection yet do not prevent sialoglycan binding. While two distinct neutralizing S1 epitopes are readily accessible in the prefusion S trimer, other sites are occluded such that their accessibility must be subject to conformational changes in S during cell-entry. While non-neutralizing antibodies were broadly reactive against a collection of natural OC43 variants, neutralizing antibodies generally displayed restricted binding breadth. Our data provide a structure-based understanding of protective immunity and adaptive evolution for this endemic coronavirus which emerged in humans long before SARS-CoV-2.

PubMed: 35614127
DOI: 10.1038/s41467-022-30658-0

実験手法

ELECTRON MICROSCOPY (3.7 Å)