7SOE

SARS-CoV-2 S B.1.617.1 kappa variant + S2X303 Global Refinement

This is a non-PDB format compatible entry.

Summary for 7SOE

• Entry DOI: 10.2210/pdb7soe/pdb
• Related: 7SO9 7SOB
• EMDB information: 25268
• Descriptor: Spike glycoprotein, S2X303 Fab light chain, S2X303 Fab heavy chain, ... (5 entities in total)
• Functional Keywords: kappa, spike, antibody, structural genomics, seattle structural genomics center for infectious disease, ssgcid, viral protein-immune system complex, viral protein/immune system
• Biological source: Severe acute respiratory syndrome coronavirus 2; More
• Total number of polymer chains: 9
• Total formula weight: 513180.80

Authors

McCallum, M.,Veesler, D.,Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2021-10-29, release date: 2021-11-17, Last modification date: 2024-11-13)

Primary citation

McCallum, M.,Walls, A.C.,Sprouse, K.R.,Bowen, J.E.,Rosen, L.E.,Dang, H.V.,De Marco, A.,Franko, N.,Tilles, S.W.,Logue, J.,Miranda, M.C.,Ahlrichs, M.,Carter, L.,Snell, G.,Pizzuto, M.S.,Chu, H.Y.,Van Voorhis, W.C.,Corti, D.,Veesler, D.
Molecular basis of immune evasion by the Delta and Kappa SARS-CoV-2 variants.
Science, 374:1621-1626, 2021

PubMed Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) transmission leads to the emergence of variants, including the B.1.617.2 (Delta) variant of concern that is causing a new wave of infections and has become globally dominant. We show that these variants dampen the in vitro potency of vaccine-elicited serum neutralizing antibodies and provide a structural framework for describing their immune evasion. Mutations in the B.1.617.1 (Kappa) and Delta spike glycoproteins abrogate recognition by several monoclonal antibodies via alteration of key antigenic sites, including remodeling of the Delta amino-terminal domain. The angiotensin-converting enzyme 2 binding affinities of the Kappa and Delta receptor binding domains are comparable to the Wuhan-Hu-1 isolate, whereas B.1.617.2+ (Delta+) exhibits markedly reduced affinity.

PubMed: 34751595
DOI: 10.1126/science.abl8506

Experimental method

ELECTRON MICROSCOPY (2.8 Å)