Author: Supasa, Piyada; Zhou, Daming; Dejnirattisai, Wanwisa; Liu, Chang; Mentzer, Alexander J.; Ginn, Helen M.; Zhao, Yuguang; Duyvesteyn, Helen M.E.; Nutalai, Rungtiwa; Tuekprakhon, Aekkachai; Wang, Beibei; Paesen, Guido C.; Slon-Campos, Jose; López-Camacho, César; Hallis, Bassam; Coombes, Naomi; Bewley, Kevin; Charlton, Sue; Walter, Thomas S.; Barnes, Eleanor; Dunachie, Susanna J.; Skelly, Donal; Lumley, Sheila F.; Baker, Natalie; Shaik, Imam; Humphries, Holly; Godwin, Kerry; Gent, Nick; Sienkiewicz, Alex; Dold, Christina; Levin, Robert; Dong, Tao; Pollard, Andrew J.; Knight, Julian C.; Klenerman, Paul; Crook, Derrick; Lambe, Teresa; Clutterbuck, Elizabeth; Bibi, Sagida; Flaxman, Amy; Bittaye, Mustapha; Belij-Rammerstorfer, Sandra; Gilbert, Sarah; Hall, David R.; Williams, Mark A.; Paterson, Neil G.; James, William; Carroll, Miles W.; Fry, Elizabeth E.; Mongkolsapaya, Juthathip; Ren, Jingshan; Stuart, David I.; Screaton, Gavin R.
Title: Reduced neutralization of SARS-CoV-2 B.1.1.7 variant by convalescent and vaccine sera Cord-id: t0zpz3hv Document date: 2021_2_18
ID: t0zpz3hv
Snippet: SARS-CoV-2 has caused over 2M deaths in little over a year. Vaccines are being deployed at scale, aiming to generate responses against the virus spike. The scale of the pandemic and error-prone virus replication is leading to the appearance of mutant viruses and potentially escape from antibody responses. Variant B.1.1.7, now dominant in the UK, with increased transmission, harbours 9 amino-acid changes in the spike, including N501Y in the ACE2 interacting-surface. We examine the ability of B.1.
Document: SARS-CoV-2 has caused over 2M deaths in little over a year. Vaccines are being deployed at scale, aiming to generate responses against the virus spike. The scale of the pandemic and error-prone virus replication is leading to the appearance of mutant viruses and potentially escape from antibody responses. Variant B.1.1.7, now dominant in the UK, with increased transmission, harbours 9 amino-acid changes in the spike, including N501Y in the ACE2 interacting-surface. We examine the ability of B.1.1.7 to evade antibody responses elicited by natural SARS-CoV-2 infection or vaccination. We map the impact of N501Y by structure/function analysis of a large panel of well-characterised monoclonal antibodies. B.1.1.7 is harder to neutralize than parental virus, compromising neutralization by some members of a major class of public antibodies through light chain contacts with residue 501. However, widespread escape from monoclonal antibodies or antibody responses generated by natural infection or vaccination was not observed.
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