biostudies-literatureUnknown116Bruhn M<h4>Background</h4>Since the onset of the COVID-19 pandemic, SARS-CoV-2 neutralising monoclonal antibodies (mAbs) are being developed for clinical use. With the appearance of new virus variants, most mAbs lost their virus-neutralising activity, highlighting the complexity of mAb development under conditions of continuous SARS-CoV-2 evolution.<h4>Methods</h4>Hamsters were treated with SARS-CoV-2 neutralising mAbs and then challenged with SARS-CoV-2. Recombinant VSV expressing the spike protein of SARS-CoV-2 was utilised in an in vitro system to select for antibody escape variants. Surface plasmon resonance measurements were performed to characterise the binding affinity and epitope of various mAbs. Fc-mediated effector functions of neutralising and non-neutralising mAb combinations were detEBioMedicine105770https://www.ebi.ac.uk/biostudies/studies/S-EPMC12148588biostudies-literatureSomatic hypermutation shapes the viral escape profile of SARS-CoV-2 neutralising antibodies.PMC12148588Salam AHinrichs IBartsch YZimmer GKalinke UMirolo MBaumgartner WReineking WMergani AOsterhaus ADMEGonzalez-Hernandez MObara MSchambach ABruhn MfalseSomatic hypermutation shapes the viral escape profile of SARS-CoV-2 neutralising antibodies.<h4>Background</h4>Since the onset of the COVID-19 pandemic, SARS-CoV-2 neutralising monoclonal antibodies (mAbs) are being developed for clinical use. With the appearance of new virus variants, most mAbs lost their virus-neutralising activity, highlighting the complexity of mAb development under conditions of continuous SARS-CoV-2 evolution.<h4>Methods</h4>Hamsters were treated with SARS-CoV-2 neutralising mAbs and then challenged with SARS-CoV-2. Recombinant VSV expressing the spike protein of SARS-CoV-2 was utilised in an in vitro system to select for antibody escape variants. Surface plasmon resonance measurements were performed to characterise the binding affinity and epitope of various mAbs. Fc-mediated effector functions of neutralising and non-neutralising mAb combinations were det2025-01-01T00:00:00Z2025 Jun2026-06-03T07:37:43.96Z2026-04-26T03:10:17.89ZS-EPMC121485884040369610.1016/j.ebiom.2025.105770