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...

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Autores principales: Jesús Arenas, Laura Catón, Tom van den Hoeven, Vincent de Maat, Juan Cruz Herrero, Jan Tommassen
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Publicado: Taylor & Francis Group 2020
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spelling oai:doaj.org-article:d78d6fcffd204bc1a4ddc09634334f272021-11-17T14:21:59ZThe outer-membrane protein MafA of Neisseria meningitidis constitutes a novel protein secretion pathway specific for the fratricide protein MafB2150-55942150-560810.1080/21505594.2020.1851940https://doaj.org/article/d78d6fcffd204bc1a4ddc09634334f272020-12-01T00:00:00Zhttp://dx.doi.org/10.1080/21505594.2020.1851940https://doaj.org/toc/2150-5594https://doaj.org/toc/2150-5608MafB 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.Jesús ArenasLaura CatónTom van den HoevenVincent de MaatJuan Cruz HerreroJan TommassenTaylor & Francis Grouparticleinterbacterial competitionmafamafbneisseriaprotein secretionsecretometoxinInfectious and parasitic diseasesRC109-216ENVirulence, Vol 11, Iss 1, Pp 1701-1715 (2020)
institution DOAJ
collection DOAJ
language EN
topic interbacterial competition
mafa
mafb
neisseria
protein secretion
secretome
toxin
Infectious and parasitic diseases
RC109-216
spellingShingle interbacterial competition
mafa
mafb
neisseria
protein secretion
secretome
toxin
Infectious and parasitic diseases
RC109-216
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
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.
format article
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
title 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_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_sort outer-membrane protein mafa of neisseria meningitidis constitutes a novel protein secretion pathway specific for the fratricide protein mafb
publisher Taylor & Francis Group
publishDate 2020
url https://doaj.org/article/d78d6fcffd204bc1a4ddc09634334f27
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