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Antigenicity of the Mu (B.1.621) and A.2.5 SARS-CoV-2 Spikes

Debashree Chatterjee, Alexandra Tauzin, Annemarie Laumaea, Shang Yu Gong, Yuxia Bo, Aurélie Guilbault, Guillaume Goyette, Catherine Bourassa, Gabrielle Gendron‐Lepage, Halima Medjahed, Jonathan Richard, Sandrine Moreira, Marceline Côté, Andrés Finzi

2022Viruses13 citationsDOIOpen Access PDF

Abstract

The rapid emergence of SARS-CoV-2 variants is fueling the recent waves of the COVID-19 pandemic. Here, we assessed ACE2 binding and antigenicity of Mu (B.1.621) and A.2.5 Spikes. Both these variants carry some mutations shared by other emerging variants. Some of the pivotal mutations such as N501Y and E484K in the receptor-binding domain (RBD) detected in B.1.1.7 (Alpha), B.1.351 (Beta) and P.1 (Gamma) are now present within the Mu variant. Similarly, the L452R mutation of B.1.617.2 (Delta) variant is present in A.2.5. In this study, we observed that these Spike variants bound better to the ACE2 receptor in a temperature-dependent manner. Pseudoviral particles bearing the Spike of Mu were similarly neutralized by plasma from vaccinated individuals than those carrying the Beta (B.1.351) and Delta (B.1.617.2) Spikes. Altogether, our results indicate the importance of measuring critical parameters such as ACE2 interaction, plasma recognition and neutralization ability of each emerging variant.

Topics & Concepts

AntigenicitySpike (software development)ReceptorMutationNeutralizationSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)VirologyCoronavirus disease 2019 (COVID-19)BiologySpike ProteinMolecular biologyVirusAntibodyGeneticsGeneMedicineInternal medicineInfectious disease (medical specialty)DiseaseManagementEconomicsSARS-CoV-2 and COVID-19 ResearchCOVID-19 Clinical Research StudiesAnimal Virus Infections Studies
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