Article
Antibody evasion by the P.1 strain of SARS-CoV-2
Registro en:
DEJNIRATTISAI, Wanwisa et al. Antibody evasion by the P.1 strain of SARS-CoV-2. Cell, n. 184, p. 2939-2954, May 2021.
1525-0016
10.1016/j.cell.2021.03.055
Autor
Dejnirattisai, Wanwisa
Zhou, Daming
Supasa, Piyada
Liu, Chang
Mentzer, Alexander J.
Gimm, Helen M.
Zhao, Yuguang
Duyvesteyn, Helen M.E
Tuekprakhon, Aekkachai
Nutalai, Rungtiwa
Wang, Beibei
López-Camacho, César
Slon-Campos, Jose
Walter, Thomas S.
Skelly, Donal
Clemens, Sue Ann Costa
Naveca, Felipe Gomes
Nascimento, Valdinete
Nascimento, Fernanda
Costa, Cristiano Fernandes da
Resende, Paola Cristina
Pauvolid-Correa, Alex
Siqueira, Marilda Agudo Mendonça Teixeira de
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 C.
Caroll, Miles W.
Klenerman, Paul
Barnes, Eleanor
Dunachie, Susanna J.
Paterson, Neil G.
Williams, Mark A.
Hall, David R.
Hulswit, Ruben J.G.
Bowden, Thomas A
Fry, Elizabeth E.
Mongkolsapaya, Juthathip
Ren, Jingshan
Stuart, David I.
Screaton, Gavin R.
Resumen
A Rede Genômica Fiocruz é formada por especialistas de todas as unidades da Fundação no país e de institutos parceiros que se empenham diariamente em gerar dados mais robustos sobre o comportamento do SARS-Cov-2 e contribuir para um melhor preparo do país no enfrentamento da pandemia em termos de diagnóstico mais precisos e vacinas eficazes. Saiba mais sobre a Rede Genômica Fiocruz em: http://www.genomahcov.fiocruz.br/ Terminating the SARS-CoV-2 pandemic relies upon pan-global vaccination. Current vaccines elicit neutral izing antibody responses to the virus spike derived from early isolates. However, new strains have emerged
with multiple mutations, including P.1 from Brazil, B.1.351 from South Africa, and B.1.1.7 from the UK (12, 10,
and 9 changes in the spike, respectively). All have mutations in the ACE2 binding site, with P.1 and B.1.351
having a virtually identical triplet (E484K, K417N/T, and N501Y), which we show confer similar increased af finity for ACE2. We show that, surprisingly, P.1 is significantly less resistant to naturally acquired or vaccine induced antibody responses than B.1.351, suggesting that changes outside the receptor-binding domain
(RBD) impact neutralization. Monoclonal antibody (mAb) 222 neutralizes all three variants despite interacting
with two of the ACE2-binding site mutations. We explain this through structural analysis and use the 222 light
chain to largely restore neutralization potency to a major class of public antibodies