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Type B CTD Proteins Secreted by the Type IX Secretion System Associate with PorP-like Proteins for Cell Surface Anchorage
The Bacteroidetes type IX secretion system (T9SS) consists of at least 20 components that translocate proteins with type A or type B C-terminal domain (CTD) signals across the outer membrane (OM). While type A CTD proteins are anchored to the cell surface via covalent linkage to the anionic lipopoly...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9143113/ https://www.ncbi.nlm.nih.gov/pubmed/35628493 http://dx.doi.org/10.3390/ijms23105681 |
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author | Gorasia, Dhana G. Seers, Christine A. Heath, Jacqueline E. Glew, Michelle D. Soleimaninejad, Hamid Butler, Catherine A. McBride, Mark J. Veith, Paul D. Reynolds, Eric C. |
author_facet | Gorasia, Dhana G. Seers, Christine A. Heath, Jacqueline E. Glew, Michelle D. Soleimaninejad, Hamid Butler, Catherine A. McBride, Mark J. Veith, Paul D. Reynolds, Eric C. |
author_sort | Gorasia, Dhana G. |
collection | PubMed |
description | The Bacteroidetes type IX secretion system (T9SS) consists of at least 20 components that translocate proteins with type A or type B C-terminal domain (CTD) signals across the outer membrane (OM). While type A CTD proteins are anchored to the cell surface via covalent linkage to the anionic lipopolysaccharide, it is still unclear how type B CTD proteins are anchored to the cell surface. Moreover, very little is known about the PorE and PorP components of the T9SS. In this study, for the first time, we identified a complex comprising the OM β-barrel protein PorP, the OM-associated periplasmic protein PorE and the type B CTD protein PG1035. Cross-linking studies supported direct interactions between PorE-PorP and PorP-PG1035. Furthermore, we show that the formation of the PorE-PorP-PG1035 complex was independent of PorU and PorV. Additionally, the Flavobacterium johnsoniae PorP-like protein, SprF, was found bound to the major gliding motility adhesin, SprB, which is also a type B CTD protein. Together, these results suggest that type B-CTD proteins may anchor to the cell surface by binding to their respective PorP-like proteins. |
format | Online Article Text |
id | pubmed-9143113 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-91431132022-05-29 Type B CTD Proteins Secreted by the Type IX Secretion System Associate with PorP-like Proteins for Cell Surface Anchorage Gorasia, Dhana G. Seers, Christine A. Heath, Jacqueline E. Glew, Michelle D. Soleimaninejad, Hamid Butler, Catherine A. McBride, Mark J. Veith, Paul D. Reynolds, Eric C. Int J Mol Sci Article The Bacteroidetes type IX secretion system (T9SS) consists of at least 20 components that translocate proteins with type A or type B C-terminal domain (CTD) signals across the outer membrane (OM). While type A CTD proteins are anchored to the cell surface via covalent linkage to the anionic lipopolysaccharide, it is still unclear how type B CTD proteins are anchored to the cell surface. Moreover, very little is known about the PorE and PorP components of the T9SS. In this study, for the first time, we identified a complex comprising the OM β-barrel protein PorP, the OM-associated periplasmic protein PorE and the type B CTD protein PG1035. Cross-linking studies supported direct interactions between PorE-PorP and PorP-PG1035. Furthermore, we show that the formation of the PorE-PorP-PG1035 complex was independent of PorU and PorV. Additionally, the Flavobacterium johnsoniae PorP-like protein, SprF, was found bound to the major gliding motility adhesin, SprB, which is also a type B CTD protein. Together, these results suggest that type B-CTD proteins may anchor to the cell surface by binding to their respective PorP-like proteins. MDPI 2022-05-19 /pmc/articles/PMC9143113/ /pubmed/35628493 http://dx.doi.org/10.3390/ijms23105681 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Gorasia, Dhana G. Seers, Christine A. Heath, Jacqueline E. Glew, Michelle D. Soleimaninejad, Hamid Butler, Catherine A. McBride, Mark J. Veith, Paul D. Reynolds, Eric C. Type B CTD Proteins Secreted by the Type IX Secretion System Associate with PorP-like Proteins for Cell Surface Anchorage |
title | Type B CTD Proteins Secreted by the Type IX Secretion System Associate with PorP-like Proteins for Cell Surface Anchorage |
title_full | Type B CTD Proteins Secreted by the Type IX Secretion System Associate with PorP-like Proteins for Cell Surface Anchorage |
title_fullStr | Type B CTD Proteins Secreted by the Type IX Secretion System Associate with PorP-like Proteins for Cell Surface Anchorage |
title_full_unstemmed | Type B CTD Proteins Secreted by the Type IX Secretion System Associate with PorP-like Proteins for Cell Surface Anchorage |
title_short | Type B CTD Proteins Secreted by the Type IX Secretion System Associate with PorP-like Proteins for Cell Surface Anchorage |
title_sort | type b ctd proteins secreted by the type ix secretion system associate with porp-like proteins for cell surface anchorage |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9143113/ https://www.ncbi.nlm.nih.gov/pubmed/35628493 http://dx.doi.org/10.3390/ijms23105681 |
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