MultiBac: from protein complex structures to synthetic viral nanosystems

The MultiBac baculovirus/insect cell expression vector system was conceived as a user-friendly, modular tool-kit for producing multiprotein complexes for structural biology applications. MultiBac has allowed the structure and function of many molecular machines to be elucidated, including previously...

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Autores principales: Pelosse, Martin, Crocker, Hannah, Gorda, Barbara, Lemaire, Paul, Rauch, Jens, Berger, Imre
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2017
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5661938/
https://www.ncbi.nlm.nih.gov/pubmed/29084535
http://dx.doi.org/10.1186/s12915-017-0447-6
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author Pelosse, Martin
Crocker, Hannah
Gorda, Barbara
Lemaire, Paul
Rauch, Jens
Berger, Imre
author_facet Pelosse, Martin
Crocker, Hannah
Gorda, Barbara
Lemaire, Paul
Rauch, Jens
Berger, Imre
author_sort Pelosse, Martin
collection PubMed
description The MultiBac baculovirus/insect cell expression vector system was conceived as a user-friendly, modular tool-kit for producing multiprotein complexes for structural biology applications. MultiBac has allowed the structure and function of many molecular machines to be elucidated, including previously inaccessible high-value drug targets. More recently, MultiBac developments have shifted to customized baculoviral genomes that are tailored for a range of applications, including synthesizing artificial proteins by genetic code expansion. We review some of these developments, including the ongoing rewiring of the MultiBac system for mammalian applications, notably CRISPR/Cas9-mediated gene editing.
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spelling pubmed-56619382017-11-01 MultiBac: from protein complex structures to synthetic viral nanosystems Pelosse, Martin Crocker, Hannah Gorda, Barbara Lemaire, Paul Rauch, Jens Berger, Imre BMC Biol Review The MultiBac baculovirus/insect cell expression vector system was conceived as a user-friendly, modular tool-kit for producing multiprotein complexes for structural biology applications. MultiBac has allowed the structure and function of many molecular machines to be elucidated, including previously inaccessible high-value drug targets. More recently, MultiBac developments have shifted to customized baculoviral genomes that are tailored for a range of applications, including synthesizing artificial proteins by genetic code expansion. We review some of these developments, including the ongoing rewiring of the MultiBac system for mammalian applications, notably CRISPR/Cas9-mediated gene editing. BioMed Central 2017-10-30 /pmc/articles/PMC5661938/ /pubmed/29084535 http://dx.doi.org/10.1186/s12915-017-0447-6 Text en © Berger et al. 2017 Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Review
Pelosse, Martin
Crocker, Hannah
Gorda, Barbara
Lemaire, Paul
Rauch, Jens
Berger, Imre
MultiBac: from protein complex structures to synthetic viral nanosystems
title MultiBac: from protein complex structures to synthetic viral nanosystems
title_full MultiBac: from protein complex structures to synthetic viral nanosystems
title_fullStr MultiBac: from protein complex structures to synthetic viral nanosystems
title_full_unstemmed MultiBac: from protein complex structures to synthetic viral nanosystems
title_short MultiBac: from protein complex structures to synthetic viral nanosystems
title_sort multibac: from protein complex structures to synthetic viral nanosystems
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5661938/
https://www.ncbi.nlm.nih.gov/pubmed/29084535
http://dx.doi.org/10.1186/s12915-017-0447-6
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