Protein Interactome Analysis of the Type IX Secretion System Identifies PorW as the Missing Link between the PorK/N Ring Complex and the Sov Translocon

The type IX secretion system (T9SS) transports cargo proteins through the outer membrane of Bacteroidetes and attaches them to the cell surface for func- tions including pathogenesis, gliding motility, and degradation of carbon sources. The T9SS comprises at least 20 different proteins and includes...

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Published inMicrobiology spectrum Vol. 10; no. 1
Main Authors Gorasia, Dhana, Lunar Silva, Ignacio, Butler, Catherine, Chabalier, Maïalène, Doan, Thierry, Cascales, E., Veith, Paul, Reynolds, Eric C
Format Journal Article
LanguageEnglish
Published American Society for Microbiology 12.01.2022
Subjects
Biochemistry, Molecular Biology
Life Sciences
Microbiology and Parasitology
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Summary:The type IX secretion system (T9SS) transports cargo proteins through the outer membrane of Bacteroidetes and attaches them to the cell surface for func- tions including pathogenesis, gliding motility, and degradation of carbon sources. The T9SS comprises at least 20 different proteins and includes several modules: the trans- envelope core module comprising the PorL/M motor and the PorK/N ring, the outer membrane Sov translocon, and the cell attachment complex. However, the spatial or- ganization of these modules is unknown. We have characterized the protein interac- tome of the Sov translocon in Porphyromonas gingivalis and identified Sov-PorV-PorA as well as Sov-PorW-PorN-PorK to be novel networks. PorW also interacted with PGN_1783 (PorD), which was required for maximum secretion efficiency. The identifi- cation of PorW as the missing link completes a continuous interaction network from the PorL/M motor to the Sov translocon, providing a pathway for cargo delivery and energy transduction from the inner membrane to the secretion pore.
ISSN:2165-0497
2165-0497