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Journal of Hazardous Materials

Journal of Hazardous Materials

IF: 12.2
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Protein nanoscaffold enables programmable nanobody-luciferase immunoassembly for sensitive and simultaneous detection of aflatoxin B1 and ochratoxin A

Published:5 October 2023 DOI: 10.1016/j.jhazmat.2023.132701 PMID: 37839380
Shaowen Wu , Jintao Xu , Wenxing Chen , Fenghua Wang , Xiaoliang Tan , Xinlu Zou , Weijie Zhou , Wenjie Huang , Yixiong Zheng , Shihua Wang , Shijuan Yan

Abstract

Mycotoxins produced by fungi can contaminate various foods and pose significant health risks. Ensuring food safety demands rapid, highly sensitive analytical techniques. One-step Bioluminescent Enzyme Immunoassays (BLEIAs) employing nanobody-nanoluciferase fusion proteins have recently garnered attention for operational simplicity and heightened sensitivity. Nevertheless, fixed nanobody:nanoluciferase ratios in fusion proteins restrict the customization and sensitivity of traditional BLEIAs. In this study, we present a Scaffold Assembly-based BLEIA (SA-BLEIA) that overcomes these limitations through the programmable conjugation of nanobodies and luciferases onto 60-meric protein nanoscaffolds using SpyTag/SpyCatcher linkages. These nanoscaffolds facilitate the adjustable coupling of anti-aflatoxin B1 and anti-ochratoxin A nanobodies with luciferases, optimizing nanobody/luciferase ratios and diversifying specificities. Compared to conventional methods, SA-BLEIA demonstrates considerably elevated sensitivity for detecting both toxins. The elevated local concentration of luciferase significantly amplifies bioluminescence intensity, permitting reduced substrate consumption and cost-effective detection. The usage of dual-nanobody conjugates facilitates the quantification or simultaneous detection of both mycotoxins in a single test with shared reagents. The assay exhibits exceptional recovery rates in spiked cereal samples, strongly correlating with outcomes from commercial ELISA kits. Overall, this adaptable, highly sensitive, cost-effective, and multiplexed immunoassay underscores the potential of tunable scaffold assembly as a promising avenue for advancing bioanalytical diagnostic tools.

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