The outer-membrane protein MafA of Neisseria meningitidis constitutes a novel protein secretion pathway specific for the fratricide protein MafB
MafB proteins are toxins secreted by Neisseria spp. which are involved in interbacterial competition. Their secretion mechanism has so far not been elucidated. Each strain can produce several MafB variants. On the chromosome, the mafB genes are localized on genomic islands also containing mafA genes...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Taylor & Francis Group
2020-12-01
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| Series: | Virulence |
| Subjects: | |
| Online Access: | http://dx.doi.org/10.1080/21505594.2020.1851940 |
| _version_ | 1819096304169517056 |
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| author | Jesús Arenas Laura Catón Tom van den Hoeven Vincent de Maat Juan Cruz Herrero Jan Tommassen |
| author_facet | Jesús Arenas Laura Catón Tom van den Hoeven Vincent de Maat Juan Cruz Herrero Jan Tommassen |
| author_sort | Jesús Arenas |
| collection | DOAJ |
| description | MafB proteins are toxins secreted by Neisseria spp. which are involved in interbacterial competition. Their secretion mechanism has so far not been elucidated. Each strain can produce several MafB variants. On the chromosome, the mafB genes are localized on genomic islands also containing mafA genes. MafA proteins have a role in virulence with reported activities in adhesion and transcytosis of pathogenic Neisseria, a priori unrelated to MafB activities. In this study, we investigated the possible involvement of MafA in the transport of MafB across the outer membrane of Neisseria meningitidis. In wild-type strains, proteolytic fragments of MafB proteins were detected in the extracellular medium. In the absence of MafA, secretion was abrogated, and, in the case of MafBI, full-length and truncated polypeptides were detected inside the cells and inside outer-membrane vesicles. MafBI secretion required its cognate MafA, whereas MafBIII could use any MafA. Heterologous expression in Escherichia coli showed that MafBIII is transported to a cell-surface-exposed, i.e. protease-accessible, location in a MafA-dependent way. MafA itself was found to be localized to the outer membrane, forming large oligomeric complexes. As homologs were found in diverse bacteria, the Maf system represents a new protein secretion system in Gram-negative bacteria. |
| first_indexed | 2024-12-21T23:57:04Z |
| format | Article |
| id | doaj.art-d78d6fcffd204bc1a4ddc09634334f27 |
| institution | Directory Open Access Journal |
| issn | 2150-5594 2150-5608 |
| language | English |
| last_indexed | 2024-12-21T23:57:04Z |
| publishDate | 2020-12-01 |
| publisher | Taylor & Francis Group |
| record_format | Article |
| series | Virulence |
| spelling | doaj.art-d78d6fcffd204bc1a4ddc09634334f272022-12-21T18:45:47ZengTaylor & Francis GroupVirulence2150-55942150-56082020-12-011111701171510.1080/21505594.2020.18519401851940The outer-membrane protein MafA of Neisseria meningitidis constitutes a novel protein secretion pathway specific for the fratricide protein MafBJesús Arenas0Laura Catón1Tom van den Hoeven2Vincent de Maat3Juan Cruz Herrero4Jan Tommassen5Utrecht UniversityUtrecht UniversityUtrecht UniversityUtrecht UniversityUtrecht UniversityUtrecht UniversityMafB proteins are toxins secreted by Neisseria spp. which are involved in interbacterial competition. Their secretion mechanism has so far not been elucidated. Each strain can produce several MafB variants. On the chromosome, the mafB genes are localized on genomic islands also containing mafA genes. MafA proteins have a role in virulence with reported activities in adhesion and transcytosis of pathogenic Neisseria, a priori unrelated to MafB activities. In this study, we investigated the possible involvement of MafA in the transport of MafB across the outer membrane of Neisseria meningitidis. In wild-type strains, proteolytic fragments of MafB proteins were detected in the extracellular medium. In the absence of MafA, secretion was abrogated, and, in the case of MafBI, full-length and truncated polypeptides were detected inside the cells and inside outer-membrane vesicles. MafBI secretion required its cognate MafA, whereas MafBIII could use any MafA. Heterologous expression in Escherichia coli showed that MafBIII is transported to a cell-surface-exposed, i.e. protease-accessible, location in a MafA-dependent way. MafA itself was found to be localized to the outer membrane, forming large oligomeric complexes. As homologs were found in diverse bacteria, the Maf system represents a new protein secretion system in Gram-negative bacteria.http://dx.doi.org/10.1080/21505594.2020.1851940interbacterial competitionmafamafbneisseriaprotein secretionsecretometoxin |
| spellingShingle | Jesús Arenas Laura Catón Tom van den Hoeven Vincent de Maat Juan Cruz Herrero Jan Tommassen The outer-membrane protein MafA of Neisseria meningitidis constitutes a novel protein secretion pathway specific for the fratricide protein MafB Virulence interbacterial competition mafa mafb neisseria protein secretion secretome toxin |
| title | The outer-membrane protein MafA of Neisseria meningitidis constitutes a novel protein secretion pathway specific for the fratricide protein MafB |
| title_full | The outer-membrane protein MafA of Neisseria meningitidis constitutes a novel protein secretion pathway specific for the fratricide protein MafB |
| title_fullStr | The outer-membrane protein MafA of Neisseria meningitidis constitutes a novel protein secretion pathway specific for the fratricide protein MafB |
| title_full_unstemmed | The outer-membrane protein MafA of Neisseria meningitidis constitutes a novel protein secretion pathway specific for the fratricide protein MafB |
| title_short | The outer-membrane protein MafA of Neisseria meningitidis constitutes a novel protein secretion pathway specific for the fratricide protein MafB |
| title_sort | outer membrane protein mafa of neisseria meningitidis constitutes a novel protein secretion pathway specific for the fratricide protein mafb |
| topic | interbacterial competition mafa mafb neisseria protein secretion secretome toxin |
| url | http://dx.doi.org/10.1080/21505594.2020.1851940 |
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