Pseudo-Luciferase Activity of the SARS-CoV-2 Spike Protein for Cypridina Luciferin,ACS Central Science

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Pseudo-Luciferase Activity of the SARS-CoV-2 Spike Protein for Cypridina Luciferin
ACS Central Science ( IF 12.7 ) Pub Date : 2024-01-17 , DOI: 10.1021/acscentsci.3c00887
Ryo Nishihara _{1,

2} , Hisham M Dokainish _{3,

4} , Yoshiki Kihara _{1,

5} , Hiroki Ashiba ₁ , Yuji Sugita _{4,

6,

7} , Ryoji Kurita _{1,

5}

Affiliation

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.

中文翻译：

SARS-CoV-2 刺突蛋白对鲤鱼荧光素的伪荧光素酶活性

涉及来自发光生物的发光底物（荧光素）和酶（荧光素酶）的酶反应能够以高特异性对目标蛋白和细胞进行发光检测，尽管传统的检测设计需要用荧光素酶对目标分子进行预标记。在这里，我们报告了一种不依赖于荧光素酶的发光测定，其中目标蛋白直接催化荧光素的氧化发光反应。 SARS-CoV-2 抗原（刺突）蛋白催化Cypridina荧光素的光发射，而唾液蛋白则没有观察到这种催化功能。这种选择性发光反应是由于在刺突蛋白单元之间的界面处对荧光素中的 3-(1-胍基)丙基进行酶促识别，从而无需样品预处理即可特异性检测人唾液中的刺突蛋白。该方法提供了一种无需基因操作或抗体即可简单快速检测病毒抗原的新平台。

更新日期：2024-01-17

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