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Efficient production of a mature and functional gamma secretase protease
Baculoviral protein expression in insect cells has been previously used to generate large quantities of a protein of interest for subsequent use in biochemical and structural analyses. The MultiBac baculovirus protein expression system has enabled, the use of a single baculovirus to reconstitute a p...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6110731/ https://www.ncbi.nlm.nih.gov/pubmed/30150752 http://dx.doi.org/10.1038/s41598-018-30788-w |
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author | Khan, Imran Krishnaswamy, Sudarsan Sabale, Miheer Groth, David Wijaya, Linda Morici, Michael Berger, Imre Schaffitzel, Christiane Fraser, Paul E. Martins, Ralph N. Verdile, Giuseppe |
author_facet | Khan, Imran Krishnaswamy, Sudarsan Sabale, Miheer Groth, David Wijaya, Linda Morici, Michael Berger, Imre Schaffitzel, Christiane Fraser, Paul E. Martins, Ralph N. Verdile, Giuseppe |
author_sort | Khan, Imran |
collection | PubMed |
description | Baculoviral protein expression in insect cells has been previously used to generate large quantities of a protein of interest for subsequent use in biochemical and structural analyses. The MultiBac baculovirus protein expression system has enabled, the use of a single baculovirus to reconstitute a protein complex of interest, resulting in a larger protein yield. Using this system, we aimed to reconstruct the gamma (γ)-secretase complex, a multiprotein enzyme complex essential for the production of amyloid-β (Aβ) protein. A MultiBac vector containing all components of the γ-secretase complex was generated and expression was observed for all components. The complex was active in processing APP and Notch derived γ-secretase substrates and proteolysis could be inhibited with γ-secretase inhibitors, confirming specificity of the recombinant γ-secretase enzyme. Finally, affinity purification was used to purify an active recombinant γ-secretase complex. In this study we demonstrated that the MultiBac protein expression system can be used to generate an active γ-secretase complex and provides a new tool to study γ-secretase enzyme and its variants. |
format | Online Article Text |
id | pubmed-6110731 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-61107312018-08-30 Efficient production of a mature and functional gamma secretase protease Khan, Imran Krishnaswamy, Sudarsan Sabale, Miheer Groth, David Wijaya, Linda Morici, Michael Berger, Imre Schaffitzel, Christiane Fraser, Paul E. Martins, Ralph N. Verdile, Giuseppe Sci Rep Article Baculoviral protein expression in insect cells has been previously used to generate large quantities of a protein of interest for subsequent use in biochemical and structural analyses. The MultiBac baculovirus protein expression system has enabled, the use of a single baculovirus to reconstitute a protein complex of interest, resulting in a larger protein yield. Using this system, we aimed to reconstruct the gamma (γ)-secretase complex, a multiprotein enzyme complex essential for the production of amyloid-β (Aβ) protein. A MultiBac vector containing all components of the γ-secretase complex was generated and expression was observed for all components. The complex was active in processing APP and Notch derived γ-secretase substrates and proteolysis could be inhibited with γ-secretase inhibitors, confirming specificity of the recombinant γ-secretase enzyme. Finally, affinity purification was used to purify an active recombinant γ-secretase complex. In this study we demonstrated that the MultiBac protein expression system can be used to generate an active γ-secretase complex and provides a new tool to study γ-secretase enzyme and its variants. Nature Publishing Group UK 2018-08-27 /pmc/articles/PMC6110731/ /pubmed/30150752 http://dx.doi.org/10.1038/s41598-018-30788-w Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Khan, Imran Krishnaswamy, Sudarsan Sabale, Miheer Groth, David Wijaya, Linda Morici, Michael Berger, Imre Schaffitzel, Christiane Fraser, Paul E. Martins, Ralph N. Verdile, Giuseppe Efficient production of a mature and functional gamma secretase protease |
title | Efficient production of a mature and functional gamma secretase protease |
title_full | Efficient production of a mature and functional gamma secretase protease |
title_fullStr | Efficient production of a mature and functional gamma secretase protease |
title_full_unstemmed | Efficient production of a mature and functional gamma secretase protease |
title_short | Efficient production of a mature and functional gamma secretase protease |
title_sort | efficient production of a mature and functional gamma secretase protease |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6110731/ https://www.ncbi.nlm.nih.gov/pubmed/30150752 http://dx.doi.org/10.1038/s41598-018-30788-w |
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