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TitleRapid escape of new SARS-CoV-2 Omicron variants from BA.2-directed antibody responses.
Journal, issue, pagesCell Rep, Vol. 42, Issue 4, Page 112271, Year 2023
Publish dateApr 25, 2023
AuthorsAiste Dijokaite-Guraliuc / Raksha Das / Daming Zhou / Helen M Ginn / Chang Liu / Helen M E Duyvesteyn / Jiandong Huo / Rungtiwa Nutalai / Piyada Supasa / Muneeswaran Selvaraj / Thushan I de Silva / Megan Plowright / Thomas A H Newman / Hailey Hornsby / Alexander J Mentzer / Donal Skelly / Thomas G Ritter / Nigel Temperton / Paul Klenerman / Eleanor Barnes / Susanna J Dunachie / / Cornelius Roemer / Thomas P Peacock / Neil G Paterson / Mark A Williams / David R Hall / Elizabeth E Fry / Juthathip Mongkolsapaya / Jingshan Ren / David I Stuart / Gavin R Screaton /
PubMed AbstractIn November 2021, Omicron BA.1, containing a raft of new spike mutations, emerged and quickly spread globally. Intense selection pressure to escape the antibody response produced by vaccines or ...In November 2021, Omicron BA.1, containing a raft of new spike mutations, emerged and quickly spread globally. Intense selection pressure to escape the antibody response produced by vaccines or severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) infection then led to a rapid succession of Omicron sub-lineages with waves of BA.2 and then BA.4/5 infection. Recently, many variants have emerged such as BQ.1 and XBB, which carry up to 8 additional receptor-binding domain (RBD) amino acid substitutions compared with BA.2. We describe a panel of 25 potent monoclonal antibodies (mAbs) generated from vaccinees suffering BA.2 breakthrough infections. Epitope mapping shows potent mAb binding shifting to 3 clusters, 2 corresponding to early-pandemic binding hotspots. The RBD mutations in recent variants map close to these binding sites and knock out or severely knock down neutralization activity of all but 1 potent mAb. This recent mAb escape corresponds with large falls in neutralization titer of vaccine or BA.1, BA.2, or BA.4/5 immune serum.
External linksCell Rep / PubMed:36995936 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.74 - 3.58 Å
Structure data

15971

8bcz

EMDB-15971, PDB-8bcz:
SARS-CoV-2 Delta-RBD complexed with Fabs BA.2-36, BA.2-23, EY6A and COVOX-45
Method: EM (single particle) / Resolution: 2.9 Å

PDB-8bbn:
SARS-CoV-2 Delta-RBD complexed with BA.2-10 and EY6A Fabs
Method: X-RAY DIFFRACTION / Resolution: 3.58 Å

PDB-8bbo:
SARS-CoV-2 Delta-RBD complexed with BA.2-36 Fab
Method: X-RAY DIFFRACTION / Resolution: 2.75 Å

PDB-8c3v:
SARS-CoV-2 Delta-RBD complexed with BA.2-13 Fab and C1 nanobody
Method: X-RAY DIFFRACTION / Resolution: 2.74 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-PG0:
2-(2-METHOXYETHOXY)ETHANOL / inhibitor, precipitant*YM / 2-(2-Methoxyethoxy)ethanol

ChemComp-PG4:
TETRAETHYLENE GLYCOL / precipitant*YM / Polyethylene glycol

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
  • lama glama (llama)
KeywordsVIRAL PROTEIN / SARS-CoV-2 / BA.2 mAb / RBD / BA.2-36 / BA.2-10 / BA.2-23 / EY6A / COVOX045 / delta / vaccine / BA.2-13 / VIRAL PROTEIN/Immune system

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