AI334 and AQ806 antibodies recognize the spike S protein from SARS-CoV-2 by ELISA

Lima, Wanessa Cristina

doi:10.1101/2020.05.08.084103

Cited by 5 publications

(4 citation statements)

References 11 publications

(3 reference statements)

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“…Indeed, we did not observe a strong response to linear peptides in the RBD. A control experiment with AI334/CR3022 antibody [25, 70] showed only weak binding to 367-378 peptide sequence of the RBD.…”

Section: Resultsmentioning

confidence: 99%

Identification of immunodominant linear epitopes from SARS-CoV-2 patient plasma

Farrera-Soler

Daguer

Barluenga

et al. 2020

Preprint

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Section: Resultsmentioning

confidence: 99%

Identification of immunodominant linear epitopes from SARS-CoV-2 patient plasma

Farrera-Soler

Daguer

Barluenga

et al. 2020

Preprint

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“…Indeed, we did not observe a strong response to linear peptides in the RBD. A control experiment with AI334/CR3022 antibody [25,71] showed only weak binding to 367-378 peptide sequence of the RBD.…”

Section: Plos Onementioning

confidence: 93%

Identification of immunodominant linear epitopes from SARS-CoV-2 patient plasma

et al. 2020

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A novel severe acute respiratory syndrome coronavirus (SARS-CoV-2) is the source of a current pandemic (COVID-19) with devastating consequences in public health and economic stability. Using a peptide array to map the antibody response of plasma from healing patients (12) and heathy patients (6), we identified three immunodominant linear epitopes, two of which correspond to key proteolytic sites on the spike protein (S1/S2 and S2') known to be critical for cellular entry. We show biochemical evidence that plasma positive for the epitope adjacent to the S1/S2 cleavage site inhibits furin-mediated proteolysis of spike.

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“…1). AI334 was used as a positive control (Hammel et al, 2020); AS273 showed no specific binding, most probably due to the fact that this antibody is poorly produced ( Table 1, Fig. 1).…”

Section: Resultsmentioning

confidence: 99%