American Chemical Society
oc3c00887_si_001.pdf (1.93 MB)

Pseudo-Luciferase Activity of the SARS-CoV‑2 Spike Protein for Cypridina Luciferin

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journal contribution
posted on 2024-01-17, 13:16 authored by Ryo Nishihara, Hisham M. Dokainish, Yoshiki Kihara, Hiroki Ashiba, Yuji Sugita, Ryoji Kurita
Enzymatic reactions that involve a luminescent substrate (luciferin) and enzyme (luciferase) from luminous organisms enable a luminescence detection of target proteins and cells with high specificity, albeit that conventional assay design requires a prelabeling of target molecules with luciferase. Here, we report a luciferase-independent luminescence assay in which the target protein directly catalyzes the oxidative luminescence reaction of luciferin. The SARS-CoV-2 antigen (spike) protein catalyzes the light emission of Cypridina luciferin, whereas no such catalytic function was observed for salivary proteins. This selective luminescence reaction is due to the enzymatic recognition of the 3-(1-guanidino)­propyl group in luciferin at the interfaces between the units of the spike protein, allowing a specific detection of the spike protein in human saliva without sample pretreatment. This method offers a novel platform to detect virus antigens simply and rapidly without genetic manipulation or antibodies.