7LWS

UK (B.1.1.7) SARS-CoV-2 S-GSAS-D614G variant spike protein in the 3-RBD-down conformation

Summary for 7LWS

• Entry DOI: 10.2210/pdb7lws/pdb
• EMDB information: 23555 23556 23557 23558 23559
• Descriptor: Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: sars-cov-2 spike protein trimer, viral protein
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV, SARS-CoV-2)
• Total number of polymer chains: 3
• Total formula weight: 439996.35

Authors

Gobeil, S.,Acharya, P. (deposition date: 2021-03-01, release date: 2021-03-31, Last modification date: 2024-11-20)

Primary citation

Gobeil, S.M.,Janowska, K.,McDowell, S.,Mansouri, K.,Parks, R.,Stalls, V.,Kopp, M.F.,Manne, K.,Saunders, K.,Edwards, R.J.,Haynes, B.F.,Henderson, R.C.,Acharya, P.
Effect of natural mutations of SARS-CoV-2 on spike structure, conformation and antigenicity.
Biorxiv, 2021

PubMed Abstract: New SARS-CoV-2 variants that have accumulated multiple mutations in the spike (S) glycoprotein enable increased transmission and resistance to neutralizing antibodies. Here, we study the antigenic and structural impacts of the S protein mutations from four variants, one that was involved in transmission between minks and humans, and three that rapidly spread in human populations and originated in the United Kingdom, Brazil or South Africa. All variants either retained or improved binding to the ACE2 receptor. The B.1.1.7 (UK) and B.1.1.28 (Brazil) spike variants showed reduced binding to neutralizing NTD and RBD antibodies, respectively, while the B.1.351 (SA) variant showed reduced binding to both NTD- and RBD-directed antibodies. Cryo-EM structural analyses revealed allosteric effects of the mutations on spike conformations and revealed mechanistic differences that either drive inter-species transmission or promotes viral escape from dominant neutralizing epitopes.

PubMed: 33758838
DOI: 10.1101/2021.03.11.435037

Experimental method

ELECTRON MICROSCOPY (3.22 Å)