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The outer-membrane export signal of Porphyromonas gingivalis type IX secretion system (T9SS) is a conserved C-terminal β-sandwich domain

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The outer-membrane export signal of Porphyromonas gingivalis type IX secretion system (T9SS) is a conserved C-terminal β-sandwich domain. / de Diego, Iñaki; Ksiazek, Miroslaw; Mizgalska, Danuta; Koneru, Lahari; Golik, Przemyslaw; Szmigielski, Borys; Nowak, Magdalena; Nowakowska, Zuzanna; Potempa, Barbara; Houston, John A; Enghild, Jan J; Thøgersen, Ida B; Gao, Jinlong; Kwan, Ann H; Trewhella, Jill; Dubin, Grzegorz; Gomis-Rüth, F Xavier; Nguyen, Ky-Anh; Potempa, Jan.

I: Scientific Reports, Bind 6, 2016, s. 23123.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

de Diego, I, Ksiazek, M, Mizgalska, D, Koneru, L, Golik, P, Szmigielski, B, Nowak, M, Nowakowska, Z, Potempa, B, Houston, JA, Enghild, JJ, Thøgersen, IB, Gao, J, Kwan, AH, Trewhella, J, Dubin, G, Gomis-Rüth, FX, Nguyen, K-A & Potempa, J 2016, 'The outer-membrane export signal of Porphyromonas gingivalis type IX secretion system (T9SS) is a conserved C-terminal β-sandwich domain', Scientific Reports, bind 6, s. 23123. https://doi.org/10.1038/srep23123

APA

de Diego, I., Ksiazek, M., Mizgalska, D., Koneru, L., Golik, P., Szmigielski, B., Nowak, M., Nowakowska, Z., Potempa, B., Houston, J. A., Enghild, J. J., Thøgersen, I. B., Gao, J., Kwan, A. H., Trewhella, J., Dubin, G., Gomis-Rüth, F. X., Nguyen, K-A., & Potempa, J. (2016). The outer-membrane export signal of Porphyromonas gingivalis type IX secretion system (T9SS) is a conserved C-terminal β-sandwich domain. Scientific Reports, 6, 23123. https://doi.org/10.1038/srep23123

CBE

de Diego I, Ksiazek M, Mizgalska D, Koneru L, Golik P, Szmigielski B, Nowak M, Nowakowska Z, Potempa B, Houston JA, Enghild JJ, Thøgersen IB, Gao J, Kwan AH, Trewhella J, Dubin G, Gomis-Rüth FX, Nguyen K-A, Potempa J. 2016. The outer-membrane export signal of Porphyromonas gingivalis type IX secretion system (T9SS) is a conserved C-terminal β-sandwich domain. Scientific Reports. 6:23123. https://doi.org/10.1038/srep23123

MLA

Vancouver

Author

de Diego, Iñaki ; Ksiazek, Miroslaw ; Mizgalska, Danuta ; Koneru, Lahari ; Golik, Przemyslaw ; Szmigielski, Borys ; Nowak, Magdalena ; Nowakowska, Zuzanna ; Potempa, Barbara ; Houston, John A ; Enghild, Jan J ; Thøgersen, Ida B ; Gao, Jinlong ; Kwan, Ann H ; Trewhella, Jill ; Dubin, Grzegorz ; Gomis-Rüth, F Xavier ; Nguyen, Ky-Anh ; Potempa, Jan. / The outer-membrane export signal of Porphyromonas gingivalis type IX secretion system (T9SS) is a conserved C-terminal β-sandwich domain. I: Scientific Reports. 2016 ; Bind 6. s. 23123.

Bibtex

@article{997268e189114f50975ae7c73c481478,
title = "The outer-membrane export signal of Porphyromonas gingivalis type IX secretion system (T9SS) is a conserved C-terminal β-sandwich domain",
abstract = "In the recently characterized Type IX Secretion System (T9SS), the conserved C-terminal domain (CTD) in secreted proteins functions as an outer membrane translocation signal for export of virulence factors to the cell surface in the Gram-negative Bacteroidetes phylum. In the periodontal pathogen Porphyromonas gingivalis, the CTD is cleaved off by PorU sortase in a sequence-independent manner, and anionic lipopolysaccharide (A-LPS) is attached to many translocated proteins, thus anchoring them to the bacterial surface. Here, we solved the atomic structure of the CTD of gingipain B (RgpB) from P. gingivalis, alone and together with a preceding immunoglobulin-superfamily domain (IgSF). The CTD was found to possess a typical Ig-like fold encompassing seven antiparallel β-strands organized in two β-sheets, packed into a β-sandwich structure that can spontaneously dimerise through C-terminal strand swapping. Small angle X-ray scattering (SAXS) revealed no fixed orientation of the CTD with respect to the IgSF. By introducing insertion or substitution of residues within the inter-domain linker in the native protein, we were able to show that despite the region being unstructured, it nevertheless is resistant to general proteolysis. These data suggest structural motifs located in the two adjacent Ig-like domains dictate the processing of CTDs by the T9SS secretion pathway.",
author = "{de Diego}, I{\~n}aki and Miroslaw Ksiazek and Danuta Mizgalska and Lahari Koneru and Przemyslaw Golik and Borys Szmigielski and Magdalena Nowak and Zuzanna Nowakowska and Barbara Potempa and Houston, {John A} and Enghild, {Jan J} and Th{\o}gersen, {Ida B} and Jinlong Gao and Kwan, {Ann H} and Jill Trewhella and Grzegorz Dubin and Gomis-R{\"u}th, {F Xavier} and Ky-Anh Nguyen and Jan Potempa",
year = "2016",
doi = "10.1038/srep23123",
language = "English",
volume = "6",
pages = "23123",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - The outer-membrane export signal of Porphyromonas gingivalis type IX secretion system (T9SS) is a conserved C-terminal β-sandwich domain

AU - de Diego, Iñaki

AU - Ksiazek, Miroslaw

AU - Mizgalska, Danuta

AU - Koneru, Lahari

AU - Golik, Przemyslaw

AU - Szmigielski, Borys

AU - Nowak, Magdalena

AU - Nowakowska, Zuzanna

AU - Potempa, Barbara

AU - Houston, John A

AU - Enghild, Jan J

AU - Thøgersen, Ida B

AU - Gao, Jinlong

AU - Kwan, Ann H

AU - Trewhella, Jill

AU - Dubin, Grzegorz

AU - Gomis-Rüth, F Xavier

AU - Nguyen, Ky-Anh

AU - Potempa, Jan

PY - 2016

Y1 - 2016

N2 - In the recently characterized Type IX Secretion System (T9SS), the conserved C-terminal domain (CTD) in secreted proteins functions as an outer membrane translocation signal for export of virulence factors to the cell surface in the Gram-negative Bacteroidetes phylum. In the periodontal pathogen Porphyromonas gingivalis, the CTD is cleaved off by PorU sortase in a sequence-independent manner, and anionic lipopolysaccharide (A-LPS) is attached to many translocated proteins, thus anchoring them to the bacterial surface. Here, we solved the atomic structure of the CTD of gingipain B (RgpB) from P. gingivalis, alone and together with a preceding immunoglobulin-superfamily domain (IgSF). The CTD was found to possess a typical Ig-like fold encompassing seven antiparallel β-strands organized in two β-sheets, packed into a β-sandwich structure that can spontaneously dimerise through C-terminal strand swapping. Small angle X-ray scattering (SAXS) revealed no fixed orientation of the CTD with respect to the IgSF. By introducing insertion or substitution of residues within the inter-domain linker in the native protein, we were able to show that despite the region being unstructured, it nevertheless is resistant to general proteolysis. These data suggest structural motifs located in the two adjacent Ig-like domains dictate the processing of CTDs by the T9SS secretion pathway.

AB - In the recently characterized Type IX Secretion System (T9SS), the conserved C-terminal domain (CTD) in secreted proteins functions as an outer membrane translocation signal for export of virulence factors to the cell surface in the Gram-negative Bacteroidetes phylum. In the periodontal pathogen Porphyromonas gingivalis, the CTD is cleaved off by PorU sortase in a sequence-independent manner, and anionic lipopolysaccharide (A-LPS) is attached to many translocated proteins, thus anchoring them to the bacterial surface. Here, we solved the atomic structure of the CTD of gingipain B (RgpB) from P. gingivalis, alone and together with a preceding immunoglobulin-superfamily domain (IgSF). The CTD was found to possess a typical Ig-like fold encompassing seven antiparallel β-strands organized in two β-sheets, packed into a β-sandwich structure that can spontaneously dimerise through C-terminal strand swapping. Small angle X-ray scattering (SAXS) revealed no fixed orientation of the CTD with respect to the IgSF. By introducing insertion or substitution of residues within the inter-domain linker in the native protein, we were able to show that despite the region being unstructured, it nevertheless is resistant to general proteolysis. These data suggest structural motifs located in the two adjacent Ig-like domains dictate the processing of CTDs by the T9SS secretion pathway.

U2 - 10.1038/srep23123

DO - 10.1038/srep23123

M3 - Journal article

C2 - 27005013

VL - 6

SP - 23123

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

ER -