Evidence of escape of SARS-CoV-2 variant B.1.351 from natural and vaccine induced sera

Zhou, Daming; Dejnirattisai, Wanwisa; Supasa, Piyada; Liu, Chang; Mentzer, Alexander J.; Ginn, Helen M.; Zhao, Yuguang; Duyvesteyn, Helen M.E.; Tuekprakhon, Aekkachai; Nutalai, Rungtiwa; Wang, Beibei; Paesen, Guido C.; Lopez-Camacho, Cesar; Slon-Campos, Jose; Hallis, Bassam; Coombes, Naomi; Bewley, Kevin; Charlton, Sue; Walter, Thomas S.; Skelly, Donal; Lumley, Sheila F.; Dold, Christina; Levin, Robert; Dong, Tao; Pollard, Andrew J.; Knight, Julian C.; Crook, Derrick; Lambe, Teresa; Clutterbuck, Elizabeth; Bibi, Sagida; Flaxman, Amy; Bittaye, Mustapha; Belij-Rammerstorfer, Sandra; Gilbert, Sarah; James, William; Carroll, Miles W.; Klenerman, Paul; Barnes, Eleanor; Dunachie, Susanna J.; Fry, Elizabeth E.; Mongkolspaya, Juthathip; Ren, Jingshan; Stuart, David I.; Screaton, Gavin R.

The race to produce vaccines against SARS-CoV-2 began when the first sequence was published, and this forms the basis for vaccines currently deployed globally. Independent lineages of SARS-CoV-2 have recently been reported: UK–B.1.1.7, South Africa–B.1.351 and Brazil–P.1. These variants have multiple changes in the immunodominant spike protein which facilitates viral cell entry via the Angiotensin converting enzyme-2 (ACE2) receptor. Mutations in the receptor recognition site on the spike are of great concern for their potential for immune escape. Here we describe a structure-function analysis of B.1.351 using a large cohort of convalescent and vaccinee serum samples. The receptor binding domain mutations provide tighter ACE2 binding and widespread escape from monoclonal antibody neutralization largely driven by E484K although K417N and N501Y act together against some important antibody classes. In a number of cases it would appear that convalescent and some vaccine serum offers limited protection against this variant.