Virotrap : trapping protein complexes in virus-like particles
- Author
- Georgios Moschonas (UGent) , Margaux De Meyer (UGent) , Delphine De Sutter (UGent) , Evy Timmerman (UGent) , Petra Van Damme (UGent) and Sven Eyckerman (UGent)
- Organization
- Abstract
- The discovery of protein-protein interactions can provide crucial information on protein function by linking proteins into known pathways or complexes within the cell. Mass spectrometry (MS)-based methods, such as affinity purification (AP)-MS and proximity-dependent biotin identification (BioID), allowed for a vast increase in the number of reported protein complexes. As a more recent addition to the arsenal of MS-based methods, Virotrap represents a unique technology that benefits from the specific properties of the human immunodeficiency virus-1 (HIV-1) Gag polyprotein. More specifically, Virotrap captures protein complexes in virus-like particles budded from human embryonic kidney (HEK293T) cells, bypassing the need for cell lysis and thus supporting identification of their content using MS. Being intrinsically different to its two main predecessors, affinity purification MS (AP-MS) and biotin-dependent identification (BioID), Virotrap was shown to complement data obtained with the existing MS-based toolkit. The proven complementarity of these MS-based strategies underlines the importance of using different techniques to enable comprehensive mapping of protein-protein interactions (PPIs). In this chapter, we provide a detailed overview of the Virotrap protocol to screen for PPIs using a bait protein of interest.
- Keywords
- Interaction network, Mass spectrometry, Protein complex, Protein-protein interaction, Virotrap
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Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-01HSXBMR78HS4YC16ZHXKWSKJC
- MLA
- Moschonas, Georgios, et al. “Virotrap : Trapping Protein Complexes in Virus-like Particles.” Mass Spectrometry-Based Proteomics, edited by Kris Gevaert, vol. 2718, Humana, 2023, pp. 53–71, doi:10.1007/978-1-0716-3457-8_4.
- APA
- Moschonas, G., De Meyer, M., De Sutter, D., Timmerman, E., Van Damme, P., & Eyckerman, S. (2023). Virotrap : trapping protein complexes in virus-like particles. In K. Gevaert (Ed.), Mass spectrometry-based proteomics (Vol. 2718, pp. 53–71). https://doi.org/10.1007/978-1-0716-3457-8_4
- Chicago author-date
- Moschonas, Georgios, Margaux De Meyer, Delphine De Sutter, Evy Timmerman, Petra Van Damme, and Sven Eyckerman. 2023. “Virotrap : Trapping Protein Complexes in Virus-like Particles.” In Mass Spectrometry-Based Proteomics, edited by Kris Gevaert, 2718:53–71. New York, NY, USA: Humana. https://doi.org/10.1007/978-1-0716-3457-8_4.
- Chicago author-date (all authors)
- Moschonas, Georgios, Margaux De Meyer, Delphine De Sutter, Evy Timmerman, Petra Van Damme, and Sven Eyckerman. 2023. “Virotrap : Trapping Protein Complexes in Virus-like Particles.” In Mass Spectrometry-Based Proteomics, ed by. Kris Gevaert, 2718:53–71. New York, NY, USA: Humana. doi:10.1007/978-1-0716-3457-8_4.
- Vancouver
- 1.Moschonas G, De Meyer M, De Sutter D, Timmerman E, Van Damme P, Eyckerman S. Virotrap : trapping protein complexes in virus-like particles. In: Gevaert K, editor. Mass spectrometry-based proteomics. New York, NY, USA: Humana; 2023. p. 53–71.
- IEEE
- [1]G. Moschonas, M. De Meyer, D. De Sutter, E. Timmerman, P. Van Damme, and S. Eyckerman, “Virotrap : trapping protein complexes in virus-like particles,” in Mass spectrometry-based proteomics, vol. 2718, K. Gevaert, Ed. New York, NY, USA: Humana, 2023, pp. 53–71.
@incollection{01HSXBMR78HS4YC16ZHXKWSKJC,
abstract = {{The discovery of protein-protein interactions can provide crucial information on protein function by linking proteins into known pathways or complexes within the cell. Mass spectrometry (MS)-based methods, such as affinity purification (AP)-MS and proximity-dependent biotin identification (BioID), allowed for a vast increase in the number of reported protein complexes. As a more recent addition to the arsenal of MS-based methods, Virotrap represents a unique technology that benefits from the specific properties of the human immunodeficiency virus-1 (HIV-1) Gag polyprotein. More specifically, Virotrap captures protein complexes in virus-like particles budded from human embryonic kidney (HEK293T) cells, bypassing the need for cell lysis and thus supporting identification of their content using MS. Being intrinsically different to its two main predecessors, affinity purification MS (AP-MS) and biotin-dependent identification (BioID), Virotrap was shown to complement data obtained with the existing MS-based toolkit. The proven complementarity of these MS-based strategies underlines the importance of using different techniques to enable comprehensive mapping of protein-protein interactions (PPIs). In this chapter, we provide a detailed overview of the Virotrap protocol to screen for PPIs using a bait protein of interest.}},
author = {{Moschonas, Georgios and De Meyer, Margaux and De Sutter, Delphine and Timmerman, Evy and Van Damme, Petra and Eyckerman, Sven}},
booktitle = {{Mass spectrometry-based proteomics}},
editor = {{Gevaert, Kris}},
isbn = {{9781071634561}},
issn = {{1064-3745}},
keywords = {{Interaction network,Mass spectrometry,Protein complex,Protein-protein interaction,Virotrap}},
language = {{eng}},
pages = {{53--71}},
publisher = {{Humana}},
series = {{Methods in molecular biology (MIMB)}},
title = {{Virotrap : trapping protein complexes in virus-like particles}},
url = {{http://doi.org/10.1007/978-1-0716-3457-8_4}},
volume = {{2718}},
year = {{2023}},
}
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