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Merck
  • Cross-reactivity of SARS-CoV structural protein antibodies against SARS-CoV-2.

Cross-reactivity of SARS-CoV structural protein antibodies against SARS-CoV-2.

bioRxiv : the preprint server for biology (2020-08-09)
Timothy A Bates, Jules B Weinstein, Scotland E Farley, Hans C Leier, William B Messer, Fikadu G Tafesse
摘要

There is currently a lack of biological tools to study the replication cycle and pathogenesis of SARS-CoV-2, the etiological agent of COVID-19. Repurposing the existing tools, including antibodies of SARS-CoV, is an effective way to accelerate the development of therapeutics for COVID-19. Here, we extensively characterized antibodies of the SARS-CoV structural proteins for their cross-reactivity, experimental utility, and neutralization of SARS-CoV-2. We assessed a total of 10 antibodies (six for Spike, two for Membrane, and one for Nucleocapsid and Envelope viral protein). We evaluated the utility of these antibodies against SARS-CoV-2 in a variety of assays, including immunofluorescence, ELISA, biolayer interferometry, western blots, and micro-neutralization. Remarkably, a high proportion of the antibodies we tested showed cross-reactivity, indicating a potentially generalizable theme of cross-reactivity between SARS-CoV and SARS-CoV-2 antibodies. These antibodies should help facilitate further research into SARS-CoV-2 basic biology. Moreover, our study provides critical information about the propensity of SARS-CoV antibodies to cross-react with SARS-CoV-2 and highlights its relevance in defining the clinical significance of such antibodies to improve testing and guide the development of novel vaccines and therapeutics.

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Sigma-Aldrich
抗-链球菌标签单克隆抗体 小鼠抗, clone GT517, affinity isolated antibody
Sigma-Aldrich
Anti-Human IgG (H+L)-Peroxidase antibody produced in donkey, affinity isolated antibody, lyophilized powder