tetano
Editor, Senior Moderator
Cell
. 2021 Feb 23;S0092-8674(21)00226-9.
doi: 10.1016/j.cell.2021.02.037. Online ahead of print.
Evidence of escape of SARS-CoV-2 variant B.1.351 from natural and vaccine-induced sera
Daming Zhou[SUP] 1 [/SUP], Wanwisa Dejnirattisai[SUP] 2 [/SUP], Piyada Supasa[SUP] 2 [/SUP], Chang Liu[SUP] 3 [/SUP], Alexander J Mentzer[SUP] 4 [/SUP], Helen M Ginn[SUP] 5 [/SUP], Yuguang Zhao[SUP] 1 [/SUP], Helen M E Duyvesteyn[SUP] 1 [/SUP], Aekkachai Tuekprakhon[SUP] 2 [/SUP], Rungtiwa Nutalai[SUP] 2 [/SUP], Beibei Wang[SUP] 2 [/SUP], Guido C Paesen[SUP] 1 [/SUP], Cesar Lopez-Camacho[SUP] 2 [/SUP], Jose Slon-Campos[SUP] 2 [/SUP], Bassam Hallis[SUP] 6 [/SUP], Naomi Coombes[SUP] 6 [/SUP], Kevin Bewley[SUP] 6 [/SUP], Sue Charlton[SUP] 6 [/SUP], Thomas S Walter[SUP] 2 [/SUP], Donal Skelly[SUP] 7 [/SUP], Sheila F Lumley[SUP] 8 [/SUP], Christina Dold[SUP] 9 [/SUP], Robert Levin[SUP] 10 [/SUP], Tao Dong[SUP] 11 [/SUP], Andrew J Pollard[SUP] 9 [/SUP], Julian C Knight[SUP] 12 [/SUP], Derrick Crook[SUP] 13 [/SUP], Teresa Lambe[SUP] 14 [/SUP], Elizabeth Clutterbuck[SUP] 9 [/SUP], Sagida Bibi[SUP] 9 [/SUP], Amy Flaxman[SUP] 14 [/SUP], Mustapha Bittaye[SUP] 14 [/SUP], Sandra Belij-Rammerstorfer[SUP] 14 [/SUP], Sarah Gilbert[SUP] 14 [/SUP], William James[SUP] 15 [/SUP], Miles W Carroll[SUP] 16 [/SUP], Paul Klenerman[SUP] 17 [/SUP], Eleanor Barnes[SUP] 17 [/SUP], Susanna J Dunachie[SUP] 18 [/SUP], Elizabeth E Fry[SUP] 1 [/SUP], Juthathip Mongkolsapaya[SUP] 19 [/SUP], Jingshan Ren[SUP] 20 [/SUP], David I Stuart[SUP] 21 [/SUP], Gavin R Screaton[SUP] 22 [/SUP]
Affiliations
Abstract
The race to produce vaccines against severe acute respiratory syndrome coronavirus 2 (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 that 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.
Keywords: ACE2; B.1.351; SARS-CoV-2; South Africa; antibody; escape; neutralization; receptor-binding domain; vaccine; variant.
. 2021 Feb 23;S0092-8674(21)00226-9.
doi: 10.1016/j.cell.2021.02.037. Online ahead of print.
Evidence of escape of SARS-CoV-2 variant B.1.351 from natural and vaccine-induced sera
Daming Zhou[SUP] 1 [/SUP], Wanwisa Dejnirattisai[SUP] 2 [/SUP], Piyada Supasa[SUP] 2 [/SUP], Chang Liu[SUP] 3 [/SUP], Alexander J Mentzer[SUP] 4 [/SUP], Helen M Ginn[SUP] 5 [/SUP], Yuguang Zhao[SUP] 1 [/SUP], Helen M E Duyvesteyn[SUP] 1 [/SUP], Aekkachai Tuekprakhon[SUP] 2 [/SUP], Rungtiwa Nutalai[SUP] 2 [/SUP], Beibei Wang[SUP] 2 [/SUP], Guido C Paesen[SUP] 1 [/SUP], Cesar Lopez-Camacho[SUP] 2 [/SUP], Jose Slon-Campos[SUP] 2 [/SUP], Bassam Hallis[SUP] 6 [/SUP], Naomi Coombes[SUP] 6 [/SUP], Kevin Bewley[SUP] 6 [/SUP], Sue Charlton[SUP] 6 [/SUP], Thomas S Walter[SUP] 2 [/SUP], Donal Skelly[SUP] 7 [/SUP], Sheila F Lumley[SUP] 8 [/SUP], Christina Dold[SUP] 9 [/SUP], Robert Levin[SUP] 10 [/SUP], Tao Dong[SUP] 11 [/SUP], Andrew J Pollard[SUP] 9 [/SUP], Julian C Knight[SUP] 12 [/SUP], Derrick Crook[SUP] 13 [/SUP], Teresa Lambe[SUP] 14 [/SUP], Elizabeth Clutterbuck[SUP] 9 [/SUP], Sagida Bibi[SUP] 9 [/SUP], Amy Flaxman[SUP] 14 [/SUP], Mustapha Bittaye[SUP] 14 [/SUP], Sandra Belij-Rammerstorfer[SUP] 14 [/SUP], Sarah Gilbert[SUP] 14 [/SUP], William James[SUP] 15 [/SUP], Miles W Carroll[SUP] 16 [/SUP], Paul Klenerman[SUP] 17 [/SUP], Eleanor Barnes[SUP] 17 [/SUP], Susanna J Dunachie[SUP] 18 [/SUP], Elizabeth E Fry[SUP] 1 [/SUP], Juthathip Mongkolsapaya[SUP] 19 [/SUP], Jingshan Ren[SUP] 20 [/SUP], David I Stuart[SUP] 21 [/SUP], Gavin R Screaton[SUP] 22 [/SUP]
Affiliations
- PMID: 33730597
- DOI: 10.1016/j.cell.2021.02.037
Abstract
The race to produce vaccines against severe acute respiratory syndrome coronavirus 2 (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 that 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.
Keywords: ACE2; B.1.351; SARS-CoV-2; South Africa; antibody; escape; neutralization; receptor-binding domain; vaccine; variant.