Publication

There's no place like OM: Vesicular sorting and secretion of the peptidylarginine deiminase of Porphyromonas gingivalis

Gabarrini, G., Palma Medina, L. M., Stobernack, T., Prins, R. C., du Teil Espina, M., Kuipers, J., Chlebowicz, M. A., Rossen, J. W. A., van Winkelhoff, A. J. & van Dijl, J. M., 5-May-2018, In : Virulence. 9, 1, p. 456-464 9 p.

Research output: Contribution to journalLetterAcademicpeer-review

APA

Gabarrini, G., Palma Medina, L. M., Stobernack, T., Prins, R. C., du Teil Espina, M., Kuipers, J., ... van Dijl, J. M. (2018). There's no place like OM: Vesicular sorting and secretion of the peptidylarginine deiminase of Porphyromonas gingivalis. Virulence, 9(1), 456-464. https://doi.org/10.1080/21505594.2017.1421827

Author

Gabarrini, Giorgio ; Palma Medina, Laura M ; Stobernack, Tim ; Prins, Rianne C ; du Teil Espina, Marines ; Kuipers, Jeroen ; Chlebowicz, Monika A ; Rossen, John W A ; van Winkelhoff, Arie Jan ; van Dijl, Jan Maarten. / There's no place like OM : Vesicular sorting and secretion of the peptidylarginine deiminase of Porphyromonas gingivalis. In: Virulence. 2018 ; Vol. 9, No. 1. pp. 456-464.

Harvard

Gabarrini, G, Palma Medina, LM, Stobernack, T, Prins, RC, du Teil Espina, M, Kuipers, J, Chlebowicz, MA, Rossen, JWA, van Winkelhoff, AJ & van Dijl, JM 2018, 'There's no place like OM: Vesicular sorting and secretion of the peptidylarginine deiminase of Porphyromonas gingivalis', Virulence, vol. 9, no. 1, pp. 456-464. https://doi.org/10.1080/21505594.2017.1421827

Standard

There's no place like OM : Vesicular sorting and secretion of the peptidylarginine deiminase of Porphyromonas gingivalis. / Gabarrini, Giorgio; Palma Medina, Laura M; Stobernack, Tim; Prins, Rianne C; du Teil Espina, Marines; Kuipers, Jeroen; Chlebowicz, Monika A; Rossen, John W A; van Winkelhoff, Arie Jan; van Dijl, Jan Maarten.

In: Virulence, Vol. 9, No. 1, 05.05.2018, p. 456-464.

Research output: Contribution to journalLetterAcademicpeer-review

Vancouver

Gabarrini G, Palma Medina LM, Stobernack T, Prins RC, du Teil Espina M, Kuipers J et al. There's no place like OM: Vesicular sorting and secretion of the peptidylarginine deiminase of Porphyromonas gingivalis. Virulence. 2018 May 5;9(1):456-464. https://doi.org/10.1080/21505594.2017.1421827


BibTeX

@article{58f1f396f63a4548b613fa5a1f5ef63c,
title = "There's no place like OM: Vesicular sorting and secretion of the peptidylarginine deiminase of Porphyromonas gingivalis",
abstract = "The oral pathogen Porphyromonas gingivalis is one of the major periodontal agents and it has been recently hailed as a potential cause of the autoimmune disease rheumatoid arthritis. In particular, the peptidylarginine deiminase enzyme of P. gingivalis (PPAD) has been implicated in the citrullination of certain host proteins and the subsequent appearance of antibodies against citrullinated proteins, which might play a role in the etiology of rheumatoid arthritis. The aim of this study was to investigate the extracellular localization of PPAD in a large panel of clinical P. gingivalis isolates. Here we show that all isolates produced PPAD. In most cases PPAD was abundantly present in secreted outer membrane vesicles (OMVs) that are massively produced by P. gingivalis, and to minor extent in a soluble secreted state. Interestingly, a small subset of clinical isolates showed drastically reduced levels of the OMV-bound PPAD and secreted most of this enzyme in the soluble state. The latter phenotype is strictly associated with a lysine residue at position 373 in PPAD, implicating the more common glutamine residue at this position in PPAD association with OMVs. Further, one isolate displayed severely restricted vesiculation. Together, our findings show for the first time that neither the major association of PPAD with vesicles, nor P. gingivalis vesiculation per se, are needed for P. gingivalis interactions with the human host.",
keywords = "PPAD, Porphyromonas gingivalis, sorting, secretion, OMVs, OM, RA, OUTER-MEMBRANE VESICLES, RHEUMATOID-ARTHRITIS, LACTOCOCCUS-LACTIS, GLIDING MOTILITY, IX SECRETION, PROTEINS, SYSTEM, PERIODONTITIS, VIRULENCE, AUTOIMMUNITY",
author = "Giorgio Gabarrini and {Palma Medina}, {Laura M} and Tim Stobernack and Prins, {Rianne C} and {du Teil Espina}, Marines and Jeroen Kuipers and Chlebowicz, {Monika A} and Rossen, {John W A} and {van Winkelhoff}, {Arie Jan} and {van Dijl}, {Jan Maarten}",
year = "2018",
month = "5",
day = "5",
doi = "10.1080/21505594.2017.1421827",
language = "English",
volume = "9",
pages = "456--464",
journal = "Virulence",
issn = "2150-5594",
publisher = "Taylor & Francis Group",
number = "1",

}

RIS

TY - JOUR

T1 - There's no place like OM

T2 - Vesicular sorting and secretion of the peptidylarginine deiminase of Porphyromonas gingivalis

AU - Gabarrini, Giorgio

AU - Palma Medina, Laura M

AU - Stobernack, Tim

AU - Prins, Rianne C

AU - du Teil Espina, Marines

AU - Kuipers, Jeroen

AU - Chlebowicz, Monika A

AU - Rossen, John W A

AU - van Winkelhoff, Arie Jan

AU - van Dijl, Jan Maarten

PY - 2018/5/5

Y1 - 2018/5/5

N2 - The oral pathogen Porphyromonas gingivalis is one of the major periodontal agents and it has been recently hailed as a potential cause of the autoimmune disease rheumatoid arthritis. In particular, the peptidylarginine deiminase enzyme of P. gingivalis (PPAD) has been implicated in the citrullination of certain host proteins and the subsequent appearance of antibodies against citrullinated proteins, which might play a role in the etiology of rheumatoid arthritis. The aim of this study was to investigate the extracellular localization of PPAD in a large panel of clinical P. gingivalis isolates. Here we show that all isolates produced PPAD. In most cases PPAD was abundantly present in secreted outer membrane vesicles (OMVs) that are massively produced by P. gingivalis, and to minor extent in a soluble secreted state. Interestingly, a small subset of clinical isolates showed drastically reduced levels of the OMV-bound PPAD and secreted most of this enzyme in the soluble state. The latter phenotype is strictly associated with a lysine residue at position 373 in PPAD, implicating the more common glutamine residue at this position in PPAD association with OMVs. Further, one isolate displayed severely restricted vesiculation. Together, our findings show for the first time that neither the major association of PPAD with vesicles, nor P. gingivalis vesiculation per se, are needed for P. gingivalis interactions with the human host.

AB - The oral pathogen Porphyromonas gingivalis is one of the major periodontal agents and it has been recently hailed as a potential cause of the autoimmune disease rheumatoid arthritis. In particular, the peptidylarginine deiminase enzyme of P. gingivalis (PPAD) has been implicated in the citrullination of certain host proteins and the subsequent appearance of antibodies against citrullinated proteins, which might play a role in the etiology of rheumatoid arthritis. The aim of this study was to investigate the extracellular localization of PPAD in a large panel of clinical P. gingivalis isolates. Here we show that all isolates produced PPAD. In most cases PPAD was abundantly present in secreted outer membrane vesicles (OMVs) that are massively produced by P. gingivalis, and to minor extent in a soluble secreted state. Interestingly, a small subset of clinical isolates showed drastically reduced levels of the OMV-bound PPAD and secreted most of this enzyme in the soluble state. The latter phenotype is strictly associated with a lysine residue at position 373 in PPAD, implicating the more common glutamine residue at this position in PPAD association with OMVs. Further, one isolate displayed severely restricted vesiculation. Together, our findings show for the first time that neither the major association of PPAD with vesicles, nor P. gingivalis vesiculation per se, are needed for P. gingivalis interactions with the human host.

KW - PPAD

KW - Porphyromonas gingivalis

KW - sorting

KW - secretion

KW - OMVs

KW - OM

KW - RA

KW - OUTER-MEMBRANE VESICLES

KW - RHEUMATOID-ARTHRITIS

KW - LACTOCOCCUS-LACTIS

KW - GLIDING MOTILITY

KW - IX SECRETION

KW - PROTEINS

KW - SYSTEM

KW - PERIODONTITIS

KW - VIRULENCE

KW - AUTOIMMUNITY

U2 - 10.1080/21505594.2017.1421827

DO - 10.1080/21505594.2017.1421827

M3 - Letter

VL - 9

SP - 456

EP - 464

JO - Virulence

JF - Virulence

SN - 2150-5594

IS - 1

ER -

ID: 55267108