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7N8I

SARS-CoV-2 S (B.1.429 / epsilon variant) + S2M11 + S2L20 (Local Refinement of the NTD/S2L20)

Summary for 7N8I
Entry DOI10.2210/pdb7n8i/pdb
EMDB information24236 24237
DescriptorS2L20 Fab Light Chain Variable Region, S2L20 Fab Heavy Chain Variable Region, Spike glycoprotein, ... (4 entities in total)
Functional Keywordscoronavirus, antibody, california, structural genomics, seattle structural genomics center for infectious disease, ssgcid, viral protein, viral protein-immune system complex, viral protein/immune system
Biological sourceHomo sapiens (Human)
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Total number of polymer chains3
Total formula weight167744.57
Authors
McCallum, M.,Seattle Structural Genomics Center for Infectious Disease (SSGCID),Veesler, D. (deposition date: 2021-06-14, release date: 2021-07-14, Last modification date: 2024-10-23)
Primary citationMcCallum, M.,Bassi, J.,De Marco, A.,Chen, A.,Walls, A.C.,Di Iulio, J.,Tortorici, M.A.,Navarro, M.J.,Silacci-Fregni, C.,Saliba, C.,Sprouse, K.R.,Agostini, M.,Pinto, D.,Culap, K.,Bianchi, S.,Jaconi, S.,Cameroni, E.,Bowen, J.E.,Tilles, S.W.,Pizzuto, M.S.,Guastalla, S.B.,Bona, G.,Pellanda, A.F.,Garzoni, C.,Van Voorhis, W.C.,Rosen, L.E.,Snell, G.,Telenti, A.,Virgin, H.W.,Piccoli, L.,Corti, D.,Veesler, D.
SARS-CoV-2 immune evasion by the B.1.427/B.1.429 variant of concern.
Science, 373:648-654, 2021
Cited by
PubMed Abstract: A novel variant of concern (VOC) named CAL.20C (B.1.427/B.1.429), which was originally detected in California, carries spike glycoprotein mutations S13I in the signal peptide, W152C in the N-terminal domain (NTD), and L452R in the receptor-binding domain (RBD). Plasma from individuals vaccinated with a Wuhan-1 isolate-based messenger RNA vaccine or from convalescent individuals exhibited neutralizing titers that were reduced 2- to 3.5-fold against the B.1.427/B.1.429 variant relative to wild-type pseudoviruses. The L452R mutation reduced neutralizing activity in 14 of 34 RBD-specific monoclonal antibodies (mAbs). The S13I and W152C mutations resulted in total loss of neutralization for 10 of 10 NTD-specific mAbs because the NTD antigenic supersite was remodeled by a shift of the signal peptide cleavage site and the formation of a new disulfide bond, as revealed by mass spectrometry and structural studies.
PubMed: 34210893
DOI: 10.1126/science.abi7994
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3 Å)
Structure validation

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