Publication

Extracellular Proteome and Citrullinome of the Oral Pathogen Porphyromonas gingivalis

Stobernack, T., Glasner, C., Junker, S., Gabarrini, G., de Smit, M., de Jong, A., Otto, A., Becher, D., van Winkelhoff, A. J. & van Dijl, J. M., Dec-2016, In : Journal of Proteome Research. 15, 12, p. 4532-4543 12 p.

Research output: Contribution to journalArticleAcademicpeer-review

APA

Stobernack, T., Glasner, C., Junker, S., Gabarrini, G., de Smit, M., de Jong, A., ... van Dijl, J. M. (2016). Extracellular Proteome and Citrullinome of the Oral Pathogen Porphyromonas gingivalis. Journal of Proteome Research, 15(12), 4532-4543. https://doi.org/10.1021/acs.jproteome.6b00634

Author

Stobernack, Tim ; Glasner, Corinna ; Junker, Sabryna ; Gabarrini, Giorgio ; de Smit, Menke ; de Jong, Anne ; Otto, Andreas ; Becher, Doerte ; van Winkelhoff, Arie Jan ; van Dijl, Jan Maarten. / Extracellular Proteome and Citrullinome of the Oral Pathogen Porphyromonas gingivalis. In: Journal of Proteome Research. 2016 ; Vol. 15, No. 12. pp. 4532-4543.

Harvard

Stobernack, T, Glasner, C, Junker, S, Gabarrini, G, de Smit, M, de Jong, A, Otto, A, Becher, D, van Winkelhoff, AJ & van Dijl, JM 2016, 'Extracellular Proteome and Citrullinome of the Oral Pathogen Porphyromonas gingivalis', Journal of Proteome Research, vol. 15, no. 12, pp. 4532-4543. https://doi.org/10.1021/acs.jproteome.6b00634

Standard

Extracellular Proteome and Citrullinome of the Oral Pathogen Porphyromonas gingivalis. / Stobernack, Tim; Glasner, Corinna; Junker, Sabryna; Gabarrini, Giorgio; de Smit, Menke; de Jong, Anne; Otto, Andreas; Becher, Doerte; van Winkelhoff, Arie Jan; van Dijl, Jan Maarten.

In: Journal of Proteome Research, Vol. 15, No. 12, 12.2016, p. 4532-4543.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

Stobernack T, Glasner C, Junker S, Gabarrini G, de Smit M, de Jong A et al. Extracellular Proteome and Citrullinome of the Oral Pathogen Porphyromonas gingivalis. Journal of Proteome Research. 2016 Dec;15(12):4532-4543. https://doi.org/10.1021/acs.jproteome.6b00634


BibTeX

@article{079ae4dcaa574ef6a82a306b844ebd82,
title = "Extracellular Proteome and Citrullinome of the Oral Pathogen Porphyromonas gingivalis",
abstract = "Porphyromonas gingivalis is an oral pathogen associated with the inflammatory disease periodontitis. Periodontitis and P. gingivalis have been associated with rheumatoid arthritis. One of the hallmarks of rheumatoid arthritis is the loss of tolerance against citrullinated proteins. Citrullination is a post translational modification of arginine residues, leading to a change in structure and function of the respective protein. This modification, which is catalyzed by peptidylarginine deiminases (PADs), plays a role in several physiological processes in the human body. Interestingly, P. gingivalis secretes a citrullinating enzyme, known as P. gingivalis PAD (PPAD), which targets bacterial and human proteins. Because the extent of P. gingivalis protein citrullination by PPAD was not yet known, the present study was aimed at identifying the extracellular proteome and citrullinome of P. gingivalis. To this end, extracellulai proteins of two reference strains, two PPAD-deficient mutants, and three clinical isolates of P. gingivalis were analyzed by mass spectrometry. The results uncovered substantial heterogeneity in the extracellular proteome and citrullinome of P. gingivalis, especially in relation to the extracellular detection of typical cytoplasmic proteins. In contrast, the major virulence factors of P. gingivalis were identified in all investigated isolates, although their citrullination was shown to vary. This may be related to post-translational processing of the PPAD enzyme. Altogether, our findings focus attention on the possible roles of 6 to 25 potentially citrullinated proteins, especially the gingipain RgpA, in periodontitis and rheumatoid arthritis.",
keywords = "Porphyromonas gingivalis, protein sorting, exoproteome, citrullination, peptidylarginine deiminase, SUBCELLULAR-LOCALIZATION PREDICTION, GRAM-NEGATIVE BACTERIA, RHEUMATOID-ARTHRITIS, PEPTIDYLARGININE DEIMINASE, STAPHYLOCOCCUS-AUREUS, BACILLUS-SUBTILIS, SIGNAL PEPTIDES, BACTEROIDES-GINGIVALIS, OUTER-MEMBRANE, VIRULENCE",
author = "Tim Stobernack and Corinna Glasner and Sabryna Junker and Giorgio Gabarrini and {de Smit}, Menke and {de Jong}, Anne and Andreas Otto and Doerte Becher and {van Winkelhoff}, {Arie Jan} and {van Dijl}, {Jan Maarten}",
year = "2016",
month = "12",
doi = "10.1021/acs.jproteome.6b00634",
language = "English",
volume = "15",
pages = "4532--4543",
journal = "Journal of Proteome Research",
issn = "1535-3893",
publisher = "NLM (Medline)",
number = "12",

}

RIS

TY - JOUR

T1 - Extracellular Proteome and Citrullinome of the Oral Pathogen Porphyromonas gingivalis

AU - Stobernack, Tim

AU - Glasner, Corinna

AU - Junker, Sabryna

AU - Gabarrini, Giorgio

AU - de Smit, Menke

AU - de Jong, Anne

AU - Otto, Andreas

AU - Becher, Doerte

AU - van Winkelhoff, Arie Jan

AU - van Dijl, Jan Maarten

PY - 2016/12

Y1 - 2016/12

N2 - Porphyromonas gingivalis is an oral pathogen associated with the inflammatory disease periodontitis. Periodontitis and P. gingivalis have been associated with rheumatoid arthritis. One of the hallmarks of rheumatoid arthritis is the loss of tolerance against citrullinated proteins. Citrullination is a post translational modification of arginine residues, leading to a change in structure and function of the respective protein. This modification, which is catalyzed by peptidylarginine deiminases (PADs), plays a role in several physiological processes in the human body. Interestingly, P. gingivalis secretes a citrullinating enzyme, known as P. gingivalis PAD (PPAD), which targets bacterial and human proteins. Because the extent of P. gingivalis protein citrullination by PPAD was not yet known, the present study was aimed at identifying the extracellular proteome and citrullinome of P. gingivalis. To this end, extracellulai proteins of two reference strains, two PPAD-deficient mutants, and three clinical isolates of P. gingivalis were analyzed by mass spectrometry. The results uncovered substantial heterogeneity in the extracellular proteome and citrullinome of P. gingivalis, especially in relation to the extracellular detection of typical cytoplasmic proteins. In contrast, the major virulence factors of P. gingivalis were identified in all investigated isolates, although their citrullination was shown to vary. This may be related to post-translational processing of the PPAD enzyme. Altogether, our findings focus attention on the possible roles of 6 to 25 potentially citrullinated proteins, especially the gingipain RgpA, in periodontitis and rheumatoid arthritis.

AB - Porphyromonas gingivalis is an oral pathogen associated with the inflammatory disease periodontitis. Periodontitis and P. gingivalis have been associated with rheumatoid arthritis. One of the hallmarks of rheumatoid arthritis is the loss of tolerance against citrullinated proteins. Citrullination is a post translational modification of arginine residues, leading to a change in structure and function of the respective protein. This modification, which is catalyzed by peptidylarginine deiminases (PADs), plays a role in several physiological processes in the human body. Interestingly, P. gingivalis secretes a citrullinating enzyme, known as P. gingivalis PAD (PPAD), which targets bacterial and human proteins. Because the extent of P. gingivalis protein citrullination by PPAD was not yet known, the present study was aimed at identifying the extracellular proteome and citrullinome of P. gingivalis. To this end, extracellulai proteins of two reference strains, two PPAD-deficient mutants, and three clinical isolates of P. gingivalis were analyzed by mass spectrometry. The results uncovered substantial heterogeneity in the extracellular proteome and citrullinome of P. gingivalis, especially in relation to the extracellular detection of typical cytoplasmic proteins. In contrast, the major virulence factors of P. gingivalis were identified in all investigated isolates, although their citrullination was shown to vary. This may be related to post-translational processing of the PPAD enzyme. Altogether, our findings focus attention on the possible roles of 6 to 25 potentially citrullinated proteins, especially the gingipain RgpA, in periodontitis and rheumatoid arthritis.

KW - Porphyromonas gingivalis

KW - protein sorting

KW - exoproteome

KW - citrullination

KW - peptidylarginine deiminase

KW - SUBCELLULAR-LOCALIZATION PREDICTION

KW - GRAM-NEGATIVE BACTERIA

KW - RHEUMATOID-ARTHRITIS

KW - PEPTIDYLARGININE DEIMINASE

KW - STAPHYLOCOCCUS-AUREUS

KW - BACILLUS-SUBTILIS

KW - SIGNAL PEPTIDES

KW - BACTEROIDES-GINGIVALIS

KW - OUTER-MEMBRANE

KW - VIRULENCE

U2 - 10.1021/acs.jproteome.6b00634

DO - 10.1021/acs.jproteome.6b00634

M3 - Article

VL - 15

SP - 4532

EP - 4543

JO - Journal of Proteome Research

JF - Journal of Proteome Research

SN - 1535-3893

IS - 12

ER -

ID: 38912071