SARS-CoV-2 Omicron XBB lineage spike structures, conformations, antigenicity, and receptor recognition.

Autor:	Zhang QE; Duke University, Duke Human Vaccine Institute, Durham, NC 27710, USA; Duke University, Department of Biochemistry, Durham, NC 27710, USA., Lindenberger J; Duke University, Duke Human Vaccine Institute, Durham, NC 27710, USA., Parsons RJ; Duke University, Duke Human Vaccine Institute, Durham, NC 27710, USA; Duke University, Department of Biochemistry, Durham, NC 27710, USA., Thakur B; Duke University, Duke Human Vaccine Institute, Durham, NC 27710, USA., Parks R; Duke University, Duke Human Vaccine Institute, Durham, NC 27710, USA., Park CS; Duke University, Duke Human Vaccine Institute, Durham, NC 27710, USA., Huang X; Duke University, Duke Human Vaccine Institute, Durham, NC 27710, USA., Sammour S; Duke University, Duke Human Vaccine Institute, Durham, NC 27710, USA., Janowska K; Duke University, Duke Human Vaccine Institute, Durham, NC 27710, USA., Spence TN; Duke University, Duke Human Vaccine Institute, Durham, NC 27710, USA., Edwards RJ; Duke University, Duke Human Vaccine Institute, Durham, NC 27710, USA; Duke University, Department of Medicine, Durham, NC 27710, USA., Martin M; Duke University, Duke Human Vaccine Institute, Durham, NC 27710, USA., Williams WB; Duke University, Duke Human Vaccine Institute, Durham, NC 27710, USA; Duke University, Department of Surgery, Durham, NC 27710, USA; Duke University, Department of Integrative Immunology, Durham, NC 27710, USA., Gobeil S; Duke University, Duke Human Vaccine Institute, Durham, NC 27710, USA; Université Laval, Institut de Biologie Intégrative et des Systèmes (IBIS), Département de biochimie, de microbiologie et de bio-informatique, Faculté des sciences et de génie, Centre de Recherche en Infectiologie de l'Université Laval, PROTEO, Le regroupement québécois de recherche sur la fonction, l'ingénierie et les applications des protéines, Québec, QC, Canada., Montefiori DC; Duke University, Duke Human Vaccine Institute, Durham, NC 27710, USA; Duke University, Department of Surgery, Durham, NC 27710, USA., Korber B; Theoretical Biology and Biophysics, Los Alamos National Laboratory, Los Alamos, NM 87545, USA; The New Mexico Consortium, Los Alamos, NM 87544, USA., Saunders KO; Duke University, Duke Human Vaccine Institute, Durham, NC 27710, USA; Duke University, Department of Surgery, Durham, NC 27710, USA; Duke University, Department of Integrative Immunology, Durham, NC 27710, USA; Department of Molecular Genetics and Microbiology, Duke University School of Medicine, Durham, NC 27710, USA., Haynes BF; Duke University, Duke Human Vaccine Institute, Durham, NC 27710, USA; Duke University, Department of Medicine, Durham, NC 27710, USA; Duke University, Department of Integrative Immunology, Durham, NC 27710, USA., Henderson R; Duke University, Duke Human Vaccine Institute, Durham, NC 27710, USA; Duke University, Department of Medicine, Durham, NC 27710, USA., Acharya P; Duke University, Duke Human Vaccine Institute, Durham, NC 27710, USA; Duke University, Department of Biochemistry, Durham, NC 27710, USA; Duke University, Department of Surgery, Durham, NC 27710, USA. Electronic address: priyamvada.acharya@duke.edu.
Jazyk:	angličtina
Zdroj:	Molecular cell [Mol Cell] 2024 Jul 25; Vol. 84 (14), pp. 2747-2764.e7.
DOI:	10.1016/j.molcel.2024.06.028
Abstrakt:	A recombinant lineage of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron variant, named XBB, appeared in late 2022 and evolved descendants that successively swept local and global populations. XBB lineage members were noted for their improved immune evasion and transmissibility. Here, we determine cryoelectron microscopy (cryo-EM) structures of XBB.1.5, XBB.1.16, EG.5, and EG.5.1 spike (S) ectodomains to reveal reinforced 3-receptor binding domain (RBD)-down receptor-inaccessible closed states mediated by interprotomer RBD interactions previously observed in BA.1 and BA.2. Improved XBB.1.5 and XBB.1.16 RBD stability compensated for stability loss caused by early Omicron mutations, while the F456L substitution reduced EG.5 RBD stability. S1 subunit mutations had long-range impacts on conformation and epitope presentation in the S2 subunit. Our results reveal continued S protein evolution via simultaneous optimization of multiple parameters, including stability, receptor binding, and immune evasion, and the dramatic effects of relatively few residue substitutions in altering the S protein conformational landscape. Competing Interests: Declaration of interests B.F.H., K.O.S., R.J.E., S.G., and P.A. are named in patents submitted on the SARS-CoV-2 monoclonal antibodies studied in this paper. (Copyright © 2024 Elsevier Inc. All rights reserved.)
Databáze:	MEDLINE
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