tetano
Editor, Senior Moderator
Cell Rep
. 2021 Jun 29;109415.
doi: 10.1016/j.celrep.2021.109415. Online ahead of print.
SARS-CoV-2 variant B.1.617 is resistant to bamlanivimab and evades antibodies induced by infection and vaccination
Markus Hoffmann[SUP] 1 [/SUP], Heike Hofmann-Winkler[SUP] 2 [/SUP], Nadine Krüger[SUP] 2 [/SUP], Amy Kempf[SUP] 3 [/SUP], Inga Nehlmeier[SUP] 2 [/SUP], Luise Graichen[SUP] 3 [/SUP], Prerna Arora[SUP] 3 [/SUP], Anzhalika Sidarovich[SUP] 3 [/SUP], Anna-Sophie Moldenhauer[SUP] 2 [/SUP], Martin S Winkler[SUP] 4 [/SUP], Sebastian Schulz[SUP] 5 [/SUP], Hans-Martin Jäck[SUP] 5 [/SUP], Metodi V Stankov[SUP] 6 [/SUP], Georg M N Behrens[SUP] 6 [/SUP], Stefan Pöhlmann[SUP] 7 [/SUP]
Affiliations
Abstract
The emergence of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants threatens efforts to contain the coronavirus disease 2019 (COVID-19) pandemic. The number of COVID-19 cases and deaths in India has risen steeply, and a SARS-CoV-2 variant, B.1.617, is believed to be responsible for many of these cases. The spike protein of B.1.617 harbors two mutations in the receptor binding domain, which interacts with the angiotensin converting enzyme 2 (ACE2) receptor and constitutes the main target of neutralizing antibodies. Therefore, we analyze whether B.1.617 is more adept in entering cells and/or evades antibody responses. B.1.617 enters two of eight cell lines tested with roughly 50% increased efficiency and is equally inhibited by two entry inhibitors. In contrast, B.1.617 is resistant against bamlanivimab, an antibody used for COVID-19 treatment. B.1.617 evades antibodies induced by infection or vaccination, although less so than the B.1.351 variant. Collectively, our study reveals that antibody evasion of B.1.617 may contribute to the rapid spread of this variant.
Keywords: B.1.617; SARS-CoV-2; antibodies; cell entry; convalescence; immune evasion; mutations; spike protein; vaccination.
. 2021 Jun 29;109415.
doi: 10.1016/j.celrep.2021.109415. Online ahead of print.
SARS-CoV-2 variant B.1.617 is resistant to bamlanivimab and evades antibodies induced by infection and vaccination
Markus Hoffmann[SUP] 1 [/SUP], Heike Hofmann-Winkler[SUP] 2 [/SUP], Nadine Krüger[SUP] 2 [/SUP], Amy Kempf[SUP] 3 [/SUP], Inga Nehlmeier[SUP] 2 [/SUP], Luise Graichen[SUP] 3 [/SUP], Prerna Arora[SUP] 3 [/SUP], Anzhalika Sidarovich[SUP] 3 [/SUP], Anna-Sophie Moldenhauer[SUP] 2 [/SUP], Martin S Winkler[SUP] 4 [/SUP], Sebastian Schulz[SUP] 5 [/SUP], Hans-Martin Jäck[SUP] 5 [/SUP], Metodi V Stankov[SUP] 6 [/SUP], Georg M N Behrens[SUP] 6 [/SUP], Stefan Pöhlmann[SUP] 7 [/SUP]
Affiliations
- PMID: 34270919
- PMCID: PMC8238662
- DOI: 10.1016/j.celrep.2021.109415
Abstract
The emergence of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants threatens efforts to contain the coronavirus disease 2019 (COVID-19) pandemic. The number of COVID-19 cases and deaths in India has risen steeply, and a SARS-CoV-2 variant, B.1.617, is believed to be responsible for many of these cases. The spike protein of B.1.617 harbors two mutations in the receptor binding domain, which interacts with the angiotensin converting enzyme 2 (ACE2) receptor and constitutes the main target of neutralizing antibodies. Therefore, we analyze whether B.1.617 is more adept in entering cells and/or evades antibody responses. B.1.617 enters two of eight cell lines tested with roughly 50% increased efficiency and is equally inhibited by two entry inhibitors. In contrast, B.1.617 is resistant against bamlanivimab, an antibody used for COVID-19 treatment. B.1.617 evades antibodies induced by infection or vaccination, although less so than the B.1.351 variant. Collectively, our study reveals that antibody evasion of B.1.617 may contribute to the rapid spread of this variant.
Keywords: B.1.617; SARS-CoV-2; antibodies; cell entry; convalescence; immune evasion; mutations; spike protein; vaccination.