SARS-CoV-2 Omicron is an immune escape variant with an altered cell entry pathway
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Abstract
Vaccines based on the spike protein of SARS-CoV-2 are a cornerstone of the public health response to COVID-19. The emergence of hypermutated, increasingly transmissible variants of concern (VOCs) threaten this strategy. Omicron (B.1.1.529), the fifth VOC to be described, harbours multiple amino acid mutations in spike, half of which lie within the receptor-binding domain. Here we demonstrate substantial evasion of neutralization by Omicron BA.1 and BA.2 variants in vitro using sera from individuals vaccinated with ChAdOx1, BNT162b2 and mRNA-1273. These data were mirrored by a substantial reduction in real-world vaccine effectiveness that was partially restored by booster vaccination. The Omicron variants BA.1 and BA.2 did not induce cell syncytia in vitro and favoured a TMPRSS2-independent endosomal entry pathway, these phenotypes mapping to distinct regions of the spike protein. Impaired cell fusion was determined by the receptor-binding domain, while endosomal entry mapped to the S2 domain. Such marked changes in antigenicity and replicative biology may underlie the rapid global spread and altered pathogenicity of the Omicron variant.
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The record
- Venue
- Nature Microbiology
- Topic
- SARS-CoV-2 and COVID-19 Research
- Field
- Medicine
- Canadian institutions
- —
- Funders
- Institute of Infection and ImmunityEngineering and Physical Sciences Research CouncilSheffield Teaching Hospitals NHS Foundation TrustNIHR Oxford Biomedical Research CentreSt George's University Hospitals NHS Foundation TrustOxford University Hospitals NHS Foundation TrustBarts Health NHS TrustGreat Ormond Street Hospital for ChildrenLiverpool University Hospitals NHS Foundation TrustNewcastle upon Tyne Hospitals NHS Foundation TrustCambridge University HospitalsCardiff UniversityUniversity of GlasgowUniversity of NottinghamNational Institute for Health Research Health Protection Research UnitUniversity of OxfordBiotechnology and Biological Sciences Research CouncilWellcome TrustNottingham University Hospitals NHS TrustUniversity College LondonImperial College Healthcare NHS TrustDirectorate for Biological SciencesImperial College LondonBournemouth UniversityUniversity of CambridgeAcademy of Medical SciencesNational Institute for Health and Care ResearchMedical Research CouncilDepartment of Health and Social CareUniversity Hospitals Birmingham NHS Foundation TrustBetsi Cadwaladr University Health BoardGreat Ormond Street Institute of Child HealthNewcastle UniversityAlan Turing InstituteKing's College LondonUniversity Hospitals of Leicester NHS TrustKing's College Hospital NHS Foundation TrustUK Research and InnovationUniversity of PortsmouthNorthumbria University
- Keywords
- EndosomeBiologyAntigenicityVirologyIn vitroNeutralizationLipid bilayer fusionViral entryImmune systemReceptorCell biologyGeneticsAntibodyVirus
- Has abstract in OpenAlex
- yes