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Expression and production of soluble Mycobacterium tuberculosis H37Rv mycosin-3

Mycobacteria encode five type VII secretion system (T7SS) or ESX for nutrient acquisition and virulence. Mycosins are membrane-anchored components of ESX with serine protease activity but an unidentified substrate range. Establishing the substrate specificity of individual mycosins will help to eluc...

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Detalles Bibliográficos
Autores principales: Fang, Zhuo, Schubert, Wolf-Dieter, Gey van Pittius, Nicolaas Claudius
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5600315/
https://www.ncbi.nlm.nih.gov/pubmed/28955852
http://dx.doi.org/10.1016/j.bbrep.2016.02.005
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author Fang, Zhuo
Schubert, Wolf-Dieter
Gey van Pittius, Nicolaas Claudius
author_facet Fang, Zhuo
Schubert, Wolf-Dieter
Gey van Pittius, Nicolaas Claudius
author_sort Fang, Zhuo
collection PubMed
description Mycobacteria encode five type VII secretion system (T7SS) or ESX for nutrient acquisition and virulence. Mycosins are membrane-anchored components of ESX with serine protease activity but an unidentified substrate range. Establishing the substrate specificity of individual mycosins will help to elucidate individual ESX functions. Mycosin-1 and -3 orthologues from two environmental mycobacterial species, Mycobacterium smegmatis and Mycobacterium thermoresistibile, have been heterologously produced, but mycosins from Mycobacterium tuberculosis (Mtb) remain to be studied. Here we describe the successful production of Mtb mycosin-3 as a first step in investigating its structure and function.
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spelling pubmed-56003152017-09-27 Expression and production of soluble Mycobacterium tuberculosis H37Rv mycosin-3 Fang, Zhuo Schubert, Wolf-Dieter Gey van Pittius, Nicolaas Claudius Biochem Biophys Rep Research Article Mycobacteria encode five type VII secretion system (T7SS) or ESX for nutrient acquisition and virulence. Mycosins are membrane-anchored components of ESX with serine protease activity but an unidentified substrate range. Establishing the substrate specificity of individual mycosins will help to elucidate individual ESX functions. Mycosin-1 and -3 orthologues from two environmental mycobacterial species, Mycobacterium smegmatis and Mycobacterium thermoresistibile, have been heterologously produced, but mycosins from Mycobacterium tuberculosis (Mtb) remain to be studied. Here we describe the successful production of Mtb mycosin-3 as a first step in investigating its structure and function. Elsevier 2016-02-06 /pmc/articles/PMC5600315/ /pubmed/28955852 http://dx.doi.org/10.1016/j.bbrep.2016.02.005 Text en © 2016 The Authors http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).
spellingShingle Research Article
Fang, Zhuo
Schubert, Wolf-Dieter
Gey van Pittius, Nicolaas Claudius
Expression and production of soluble Mycobacterium tuberculosis H37Rv mycosin-3
title Expression and production of soluble Mycobacterium tuberculosis H37Rv mycosin-3
title_full Expression and production of soluble Mycobacterium tuberculosis H37Rv mycosin-3
title_fullStr Expression and production of soluble Mycobacterium tuberculosis H37Rv mycosin-3
title_full_unstemmed Expression and production of soluble Mycobacterium tuberculosis H37Rv mycosin-3
title_short Expression and production of soluble Mycobacterium tuberculosis H37Rv mycosin-3
title_sort expression and production of soluble mycobacterium tuberculosis h37rv mycosin-3
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5600315/
https://www.ncbi.nlm.nih.gov/pubmed/28955852
http://dx.doi.org/10.1016/j.bbrep.2016.02.005
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