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  Convenient site-selective protein coupling from bacterial raw lysates to coenzyme A-modified tobacco mosaic virus (TMV) by Bacillus subtilis Sfp phosphopantetheinyl transferase

Geiger, F., Wendlandt, T., Berking, T., Spatz, J. P., & Wege, C. (2023). Convenient site-selective protein coupling from bacterial raw lysates to coenzyme A-modified tobacco mosaic virus (TMV) by Bacillus subtilis Sfp phosphopantetheinyl transferase. Virology, 578, 61-70. doi:10.1016/j.virol.2022.11.013.

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Virology_578_2023_61_Suppl.pdf (Supplementary material), 115KB
 
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 Creators:
Geiger, Fania1, Author           
Wendlandt, Tim, Author
Berking, Tim, Author
Spatz, Joachim P.1, Author           
Wege, Christina, Author
Affiliations:
1Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              

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Free keywords: Biosensor; Enzymatic coupling; Luciferase; Phosphopantetheinyl transferase Sfp; Tobacco mosaic virus
 Abstract: A facile enzyme-mediated strategy enables site-specific covalent one-step coupling of genetically tagged luciferase molecules to coenzyme A-modified tobacco mosaic virus (TMV-CoA) both in solution and on solid supports. Bacillus subtilis surfactin phosphopantetheinyl transferase Sfp produced in E. coli mediated the conjugation of firefly luciferase N-terminally extended by eleven amino acids forming a 'ybbR tag' as Sfp-selective substrate, which even worked in bacterial raw lysates. The enzymes displayed on the protein coat of the TMV nanocarriers exhibited high activity. As TMV has proven a beneficial high surface-area adapter template stabilizing enzymes in different biosensing layouts in recent years, the use of TMV-CoA for fishing ybbR-tagged proteins from complex mixtures might become an advantageous concept for the versatile equipment of miniaturized devices with biologically active proteins. It comes along with new opportunities for immobilizing multiple functionalities on TMV adapter coatings, as desired, e.g., in handheld systems for point-of-care detection.

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Language(s): eng - English
 Dates: 2022-11-222022-08-312022-11-222022-11-262023-01
 Publication Status: Issued
 Pages: 10
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Virology
Source Genre: Journal
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Publ. Info: Orlando, Fla. : Academic Press
Pages: - Volume / Issue: 578 Sequence Number: - Start / End Page: 61 - 70 Identifier: ISSN: 0042-6822
CoNE: https://pure.mpg.de/cone/journals/resource/954922647063