Mycosins of the Mycobacterial Type VII ESX Secretion System: the Glue That Holds the Party Together
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Since their discovery as important determinants of virulence and growth, the type VII ESX secretion systems (ESX-1 to ESX-5) of slow-growing pathogenic mycobacteria have been the focus of intense scrutiny. Genetic studies have been instrumental in identifying the core components and substrates of these molecular secretion machines and have helped uncover the multifunctional properties of some of them. For instance, the mycosin MycP 1 of ESX-1, a membrane-associated subtilisin-like serine protease, was shown to have dual functions: the entire protein is essential for ESX-1 function, but only the serine protease regulates secretion activity. MycP 5 of ESX-5, on the other hand, is required for ESX-5 secretion activity, but the function of its predicted serine protease remains unknown. Recently, van Winden and colleagues (mBio 7:e01471-16, 2016, http://dx.doi.org/10.1128/mBio.01471-16 ) reported compelling evidence that MycP 1 and MycP 5 serve to stabilize the interactions of core ESX-1 and ESX-5 components, respectively, thus explaining how they facilitate the secretion activities of their associated systems.
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Different proteins, such as EspA, EspC, EspD, and EccA1, may be essential to contributing to secretion and stabilizing the core ESX/T7S complex in the case of ESX-1.
“Moreover, different proteins, such as EspA, EspC, EspD, and EccA1, may be essential to contributing to secretion and stabilizing the core ESX/T7S complex in the case of ESX-1 (44)(45)(46)(47).”
From ESX/Type VII Secretion Systems—An Important Way Out for Mycobacterial Proteins (2019) · cites this paper as [46]
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ESX/Type VII Secretion Systems—An Important Way Out for Mycobacterial Proteins
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- Authors
- Chen, J. M.
- Affiliations
- University of Saskatchewan (CA)
- Corresponding author
- Chen, Jeffrey M.
- ORCID
- Chen, Jeffrey M.
- Venue
- mBio
- Publisher
- American Society for Microbiology
- Published
- 2016-12-30
- Volume
- 7
- Issue
- 6
- ISSN
- 2150-7511 (ISSN-L)
- 2161-2129
- PMC
- PMC5156307
- OpenAlex
- W2564646617
- Cited by
- 10
- References
- 15
- Citations by year
- 2026: 1 · 2024: 1 · 2023: 1 · 2022: 1 · 2021: 1 · 2019: 4 · 2017: 1
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- mBio (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- Banting Research Foundation
- Environment and Climate Change Canada
- Natural Sciences and Engineering Research Council of Canada
- Topics
- Health Sciences › Medicine › Infectious Diseases › Tuberculosis Research and Epidemiology
- Health Sciences › Medicine › Epidemiology › Mycobacterium research and diagnosis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- Mycobacterium, ESX-1, subtilisin-like protease, protein-protein interaction, virulence factors, slow-growing mycobacteria
- MeSH terms
- Type VII Secretion Systems, Adhesives, Bacterial Proteins, Mycobacterium tuberculosis, Serine Proteases
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