{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,24]],"date-time":"2026-10-24T14:35:51Z","timestamp":1792852551352,"version":"4.5.0"},"update-to":[{"DOI":"10.1371\/journal.ppat.1007773","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2019,5,31]],"date-time":"2019-05-31T00:00:00Z","timestamp":1559260800000}}],"reference-count":80,"publisher":"Public Library of Science (PLoS)","issue":"5","license":[{"start":{"date-parts":[[2019,5,20]],"date-time":"2019-05-20T00:00:00Z","timestamp":1558310400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"The National Science Center, Poland","award":["UMO-2016\/22\/E\/NZ6\/00336"],"award-info":[{"award-number":["UMO-2016\/22\/E\/NZ6\/00336"]}]},{"name":"The National Science Center, Poland","award":["UMO-2015\/19\/D\/ST4\/01964"],"award-info":[{"award-number":["UMO-2015\/19\/D\/ST4\/01964"]}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"crossref","award":["DE022597"],"award-info":[{"award-number":["DE022597"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["DE026280"],"award-info":[{"award-number":["DE026280"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001659","name":"the Deutsche Forschungsgemeinschaft","doi-asserted-by":"crossref","award":["LE2621\/6-1"],"award-info":[{"award-number":["LE2621\/6-1"]}],"id":[{"id":"10.13039\/501100001659","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"DOI":"10.1371\/journal.ppat.1007773","type":"journal-article","created":{"date-parts":[[2019,5,20]],"date-time":"2019-05-20T17:36:22Z","timestamp":1558373782000},"page":"e1007773","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":92,"title":["Triggering NETosis via protease-activated receptor (PAR)-2 signaling as a mechanism of hijacking neutrophils function for pathogen benefits"],"prefix":"10.1371","volume":"15","author":[{"given":"Danuta","family":"Bryzek","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Izabela","family":"Ciaston","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ewelina","family":"Dobosz","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3172-4901","authenticated-orcid":true,"given":"Anna","family":"Gasiorek","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anna","family":"Makarska","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michal","family":"Sarna","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4619-2461","authenticated-orcid":true,"given":"Sigrun","family":"Eick","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Magdalena","family":"Puklo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4293-2733","authenticated-orcid":true,"given":"Maciej","family":"Lech","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Barbara","family":"Potempa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jan","family":"Potempa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3436-6425","authenticated-orcid":true,"given":"Joanna","family":"Koziel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2019,5,20]]},"reference":[{"issue":"5663","key":"ref1","doi-asserted-by":"crossref","first-page":"1532","DOI":"10.1126\/science.1092385","article-title":"Neutrophil extracellular traps kill bacteria","volume":"303","author":"V Brinkmann","year":"2004","journal-title":"Science"},{"issue":"12","key":"ref2","doi-asserted-by":"crossref","first-page":"7413","DOI":"10.4049\/jimmunol.1000675","article-title":"A novel mechanism of rapid nuclear neutrophil extracellular trap formation in response to Staphylococcus aureus","volume":"185","author":"FH Pilsczek","year":"2010","journal-title":"J Immunol"},{"issue":"11","key":"ref3","doi-asserted-by":"crossref","first-page":"e1005987","DOI":"10.1371\/journal.ppat.1005987","article-title":"Swimming Motility Mediates the Formation of Neutrophil Extracellular Traps Induced by Flagellated Pseudomonas aeruginosa","volume":"12","author":"M Floyd","year":"2016","journal-title":"PLoS Pathog"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"484","DOI":"10.3389\/fimmu.2016.00484","article-title":"Neutrophils Discriminate between Lipopolysaccharides of Different Bacterial Sources and Selectively Release Neutrophil Extracellular Traps","volume":"7","author":"E Pieterse","year":"2016","journal-title":"Front Immunol"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"37252","DOI":"10.1038\/srep37252","article-title":"Neutrophil extracellular traps are indirectly triggered by lipopolysaccharide and contribute to acute lung injury","volume":"6","author":"S Liu","year":"2016","journal-title":"Sci Rep"},{"issue":"3","key":"ref6","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1159\/000203645","article-title":"M1 protein allows Group A streptococcal survival in phagocyte extracellular traps through cathelicidin inhibition","volume":"1","author":"X Lauth","year":"2009","journal-title":"J Innate Immun"},{"issue":"12","key":"ref7","doi-asserted-by":"crossref","first-page":"6022","DOI":"10.4049\/jimmunol.1301821","article-title":"Staphylococcus aureus leukotoxin GH promotes formation of neutrophil extracellular traps","volume":"191","author":"N Malachowa","year":"2013","journal-title":"J Immunol"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"1404","DOI":"10.3389\/fimmu.2017.01404","article-title":"Janus-Faced Neutrophil Extracellular Traps in Periodontitis","volume":"8","author":"L Vitkov","year":"2017","journal-title":"Front Immunol"},{"issue":"12","key":"ref9","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1038\/s41579-018-0089-x","article-title":"The oral microbiota: dynamic communities and host interactions","volume":"16","author":"RJ Lamont","year":"2018","journal-title":"Nature reviews Microbiology"},{"issue":"4","key":"ref10","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1007\/s00784-003-0236-1","article-title":"Oral microbial biofilms and plaque-related diseases: microbial communities and their role in the shift from oral health to disease","volume":"7","author":"L Sbordone","year":"2003","journal-title":"Clin Oral Investig"},{"issue":"8","key":"ref11","doi-asserted-by":"crossref","first-page":"464","DOI":"10.1111\/j.1600-0765.1999.tb02282.x","article-title":"Molecular genetics and nomenclature of proteases of Porphyromonas gingivalis","volume":"34","author":"MA Curtis","year":"1999","journal-title":"J Periodontal Res"},{"issue":"3\u20134","key":"ref12","first-page":"223","article-title":"Titration and mapping of the active site of cysteine proteinases from Porphyromonas gingivalis (gingipains) using peptidyl chloromethanes","volume":"378","author":"J Potempa","year":"1997","journal-title":"Biol Chem"},{"issue":"7","key":"ref13","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1902\/jop.2011.100565","article-title":"Comparison of gingival crevicular fluid sampling methods in patients with severe chronic periodontitis","volume":"82","author":"A Guentsch","year":"2011","journal-title":"J Periodontol"},{"issue":"4","key":"ref14","doi-asserted-by":"crossref","first-page":"1176","DOI":"10.1128\/IAI.63.4.1176-1182.1995","article-title":"The multiple forms of trypsin-like activity present in various strains of Porphyromonas gingivalis are due to the presence of either Arg-gingipain or Lys-gingipain","volume":"63","author":"J Potempa","year":"1995","journal-title":"Infect Immun"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.archoralbio.2016.05.016","article-title":"PAI-2\/SerpinB2 inhibits proteolytic activity in a P. gingivalis-dominated multispecies bacterial consortium","volume":"70","author":"J Neilands","year":"2016","journal-title":"Arch Oral Biol"},{"issue":"2","key":"ref16","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1159\/000181144","article-title":"Corruption of innate immunity by bacterial proteases","volume":"1","author":"J Potempa","year":"2009","journal-title":"J Innate Immun"},{"issue":"4","key":"ref17","doi-asserted-by":"crossref","first-page":"471","DOI":"10.2217\/fmb.09.18","article-title":"The gingipains: scissors and glue of the periodontal pathogen, Porphyromonas gingivalis","volume":"4","author":"RE Fitzpatrick","year":"2009","journal-title":"Future Microbiol"},{"issue":"6","key":"ref18","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1016\/j.chom.2014.05.012","article-title":"Porphyromonas gingivalis manipulates complement and TLR signaling to uncouple bacterial clearance from inflammation and promote dysbiosis","volume":"15","author":"T Maekawa","year":"2014","journal-title":"Cell Host Microbe"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1186\/s12866-014-0258-7","article-title":"Role of Porphyromonas gingivalis gingipains in multi-species biofilm formation","volume":"14","author":"K Bao","year":"2014","journal-title":"BMC Microbiol"},{"issue":"Suppl 11","key":"ref20","doi-asserted-by":"crossref","first-page":"44","DOI":"10.1111\/j.1600-051X.2010.01682.x","article-title":"Working Group 2 of Seventh European Workshop on P. Host-response: understanding the cellular and molecular mechanisms of host-microbial interactions\u2014consensus of the Seventh European Workshop on Periodontology","volume":"38","author":"DF Kinane","year":"2011","journal-title":"J Clin Periodontol"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"56","DOI":"10.1159\/000329672","article-title":"Neutrophils in periodontal inflammation","volume":"15","author":"DA Scott","year":"2012","journal-title":"Front Oral Biol"},{"issue":"1","key":"ref22","doi-asserted-by":"crossref","first-page":"25","DOI":"10.3109\/01913120903419989","article-title":"Neutrophil fate in gingival crevicular fluid","volume":"34","author":"L Vitkov","year":"2010","journal-title":"Ultrastruct Pathol"},{"issue":"5","key":"ref23","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1111\/j.1600-0765.2008.01175.x","article-title":"Extracellular neutrophil traps in periodontitis","volume":"44","author":"L Vitkov","year":"2009","journal-title":"J Periodontal Res"},{"issue":"4","key":"ref24","doi-asserted-by":"crossref","first-page":"226","DOI":"10.3109\/01913121003725721","article-title":"Fibrin mimics neutrophil extracellular traps in SEM","volume":"34","author":"WD Krautgartner","year":"2010","journal-title":"Ultrastruct Pathol"},{"issue":"4","key":"ref25","doi-asserted-by":"crossref","first-page":"e18679","DOI":"10.1371\/journal.pone.0018679","article-title":"Porphyromonas gingivalis participates in pathogenesis of human abdominal aortic aneurysm by neutrophil activation. Proof of concept in rats","volume":"6","author":"S Delbosc","year":"2011","journal-title":"PLoS One"},{"issue":"6","key":"ref26","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1038\/nm.1959","article-title":"Netting neutrophils in autoimmune small-vessel vasculitis","volume":"15","author":"K Kessenbrock","year":"2009","journal-title":"Nat Med"},{"issue":"1","key":"ref27","doi-asserted-by":"crossref","first-page":"538","DOI":"10.4049\/jimmunol.1100450","article-title":"Netting neutrophils induce endothelial damage, infiltrate tissues, and expose immunostimulatory molecules in systemic lupus erythematosus","volume":"187","author":"E Villanueva","year":"2011","journal-title":"J Immunol"},{"issue":"178","key":"ref28","doi-asserted-by":"crossref","DOI":"10.1126\/scitranslmed.3005580","article-title":"NETs are a source of citrullinated autoantigens and stimulate inflammatory responses in rheumatoid arthritis","volume":"5","author":"R Khandpur","year":"2013","journal-title":"Sci Transl Med"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"81","DOI":"10.3389\/fimmu.2017.00081","article-title":"Neutrophil Extracellular Traps and Its Implications in Inflammation: An Overview","volume":"8","author":"V Delgado-Rizo","year":"2017","journal-title":"Front Immunol"},{"issue":"5","key":"ref30","doi-asserted-by":"crossref","first-page":"2420","DOI":"10.1021\/pr401227e","article-title":"Porphyromonas gingivalis outer membrane vesicles exclusively contain outer membrane and periplasmic proteins and carry a cargo enriched with virulence factors","volume":"13","author":"PD Veith","year":"2014","journal-title":"J Proteome Res"},{"issue":"3","key":"ref31","doi-asserted-by":"crossref","first-page":"677","DOI":"10.1083\/jcb.201006052","article-title":"Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps","volume":"191","author":"V Papayannopoulos","year":"2010","journal-title":"J Cell Biol"},{"issue":"6","key":"ref32","doi-asserted-by":"crossref","first-page":"1599","DOI":"10.1124\/mol.104.004366","article-title":"Suppression of pathogenicity of Porphyromonas gingivalis by newly developed gingipain inhibitors","volume":"66","author":"T Kadowaki","year":"2004","journal-title":"Mol Pharmacol"},{"issue":"9","key":"ref33","doi-asserted-by":"crossref","first-page":"2817","DOI":"10.1073\/pnas.1414055112","article-title":"SK3 channel and mitochondrial ROS mediate NADPH oxidase-independent NETosis induced by calcium influx","volume":"112","author":"DN Douda","year":"2015","journal-title":"Proceedings of the National Academy of Sciences of the United States of America"},{"issue":"3","key":"ref34","doi-asserted-by":"crossref","first-page":"532","DOI":"10.1002\/jcb.24391","article-title":"Reactive oxygen species-induced activation of ERK and p38 MAPK mediates PMA-induced NETs release from human neutrophils","volume":"114","author":"RS Keshari","year":"2013","journal-title":"J Cell Biochem"},{"issue":"1","key":"ref35","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/S0014-5793(98)01036-9","article-title":"Cleavage and activation of proteinase-activated receptor-2 on human neutrophils by gingipain-R from Porphyromonas gingivalis","volume":"435","author":"A Lourbakos","year":"1998","journal-title":"FEBS Lett"},{"issue":"8","key":"ref36","doi-asserted-by":"crossref","first-page":"5121","DOI":"10.1128\/IAI.69.8.5121-5130.2001","article-title":"Arginine-specific protease from Porphyromonas gingivalis activates protease-activated receptors on human oral epithelial cells and induces interleukin-6 secretion","volume":"69","author":"A Lourbakos","year":"2001","journal-title":"Infect Immun"},{"issue":"12","key":"ref37","doi-asserted-by":"crossref","first-page":"3790","DOI":"10.1182\/blood.V97.12.3790","article-title":"Activation of protease-activated receptors by gingipains from Porphyromonas gingivalis leads to platelet aggregation: a new trait in microbial pathogenicity","volume":"97","author":"A Lourbakos","year":"2001","journal-title":"Blood"},{"issue":"5","key":"ref38","doi-asserted-by":"crossref","first-page":"1181","DOI":"10.1111\/j.1462-5822.2008.01119.x","article-title":"Gingipains from Porphyromonas gingivalis synergistically induce the production of proinflammatory cytokines through protease-activated receptors with Toll-like receptor and NOD1\/2 ligands in human monocytic cells","volume":"10","author":"A Uehara","year":"2008","journal-title":"Cell Microbiol"},{"issue":"5","key":"ref39","doi-asserted-by":"crossref","first-page":"1217","DOI":"10.1021\/acschembio.6b01088","article-title":"Biased Signaling by Agonists of Protease Activated Receptor 2","volume":"12","author":"Y Jiang","year":"2017","journal-title":"ACS Chem Biol"},{"issue":"28","key":"ref40","doi-asserted-by":"crossref","first-page":"24638","DOI":"10.1074\/jbc.M110.201988","article-title":"Neutrophil elastase acts as a biased agonist for proteinase-activated receptor-2 (PAR2)","volume":"286","author":"R Ramachandran","year":"2011","journal-title":"J Biol Chem"},{"issue":"3","key":"ref41","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1586\/14737167.7.3.251","article-title":"Economic evaluations of human papillomavirus vaccines","volume":"7","author":"VB R","year":"2007","journal-title":"Expert Rev Pharmacoecon Outcomes Res"},{"issue":"5","key":"ref42","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/j.chom.2010.10.005","article-title":"Statins enhance formation of phagocyte extracellular traps","volume":"8","author":"OA Chow","year":"2010","journal-title":"Cell Host Microbe"},{"issue":"8","key":"ref43","doi-asserted-by":"crossref","first-page":"775","DOI":"10.1007\/s00109-009-0481-0","article-title":"Innate immunity turned inside-out: antimicrobial defense by phagocyte extracellular traps","volume":"87","author":"M von Kockritz-Blickwede","year":"2009","journal-title":"J Mol Med (Berl)"},{"issue":"4","key":"ref44","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1007\/s00430-009-0121-x","article-title":"The clinical value of neutrophil extracellular traps","volume":"198","author":"T Logters","year":"2009","journal-title":"Med Microbiol Immunol"},{"issue":"4","key":"ref45","doi-asserted-by":"crossref","first-page":"513","DOI":"10.1007\/s00281-013-0384-6","article-title":"Molecular mechanisms regulating NETosis in infection and disease","volume":"35","author":"N Branzk","year":"2013","journal-title":"Semin Immunopathol"},{"issue":"1","key":"ref46","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1111\/prd.12025","article-title":"Neutrophil extracellular traps as a new paradigm in innate immunity: friend or foe?","volume":"63","author":"PR Cooper","year":"2013","journal-title":"Periodontol 2000"},{"issue":"1","key":"ref47","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1177\/0022034515609097","article-title":"Neutrophil Extracellular Traps in Periodontitis: A Web of Intrigue","volume":"95","author":"PC White","year":"2016","journal-title":"J Dent Res"},{"issue":"5","key":"ref48","doi-asserted-by":"crossref","first-page":"361","DOI":"10.1111\/omi.12099","article-title":"The role of phagocytosis, oxidative burst and neutrophil extracellular traps in the interaction between neutrophils and the periodontal pathogen Porphyromonas gingivalis","volume":"30","author":"K Jayaprakash","year":"2015","journal-title":"Mol Oral Microbiol"},{"issue":"26","key":"ref49","doi-asserted-by":"crossref","DOI":"10.1126\/sciimmunol.aar6689","article-title":"Gasdermin D plays a vital role in the generation of neutrophil extracellular traps","volume":"3","author":"G Sollberger","year":"2018","journal-title":"Science immunology"},{"issue":"26","key":"ref50","article-title":"Noncanonical inflammasome signaling elicits gasdermin D-dependent neutrophil extracellular traps","volume":"3","author":"KW Chen","year":"2018","journal-title":"Science immunology"},{"issue":"1","key":"ref51","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1080\/21505594.2018.1454171","article-title":"Porphyromonas gingivalis traffics into endoplasmic reticulum-rich-autophagosomes for successful survival in human gingival epithelial cells","volume":"9","author":"K Lee","year":"2018","journal-title":"Virulence"},{"issue":"1","key":"ref52","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1038\/sj.cdd.4401927","article-title":"A new insight into phagocytosis of apoptotic cells: proteolytic enzymes divert the recognition and clearance of polymorphonuclear leukocytes by macrophages","volume":"14","author":"K Guzik","year":"2007","journal-title":"Cell Death Differ"},{"issue":"5","key":"ref53","doi-asserted-by":"crossref","first-page":"2647","DOI":"10.4049\/jimmunol.1300436","article-title":"Macrophage clearance of neutrophil extracellular traps is a silent process","volume":"191","author":"C Farrera","year":"2013","journal-title":"J Immunol"},{"issue":"6","key":"ref54","doi-asserted-by":"crossref","first-page":"443","DOI":"10.2174\/1389203033487027","article-title":"The biphasic virulence activities of gingipains: activation and inactivation of host proteins","volume":"4","author":"T Imamura","year":"2003","journal-title":"Curr Protein Pept Sci"},{"issue":"Pt 10","key":"ref55","doi-asserted-by":"crossref","first-page":"3238","DOI":"10.1099\/mic.0.029132-0","article-title":"Cleavage of protease-activated receptors on an immortalized oral epithelial cell line by Porphyromonas gingivalis gingipains","volume":"155","author":"RA Giacaman","year":"2009","journal-title":"Microbiology"},{"issue":"4","key":"ref56","doi-asserted-by":"crossref","first-page":"1189","DOI":"10.2353\/ajpath.2006.050658","article-title":"Protease-activated receptor-2 activation: a major role in the pathogenesis of Porphyromonas gingivalis infection","volume":"168","author":"M Holzhausen","year":"2006","journal-title":"The American journal of pathology"},{"issue":"10","key":"ref57","doi-asserted-by":"crossref","first-page":"5740","DOI":"10.1128\/IAI.70.10.5740-5750.2002","article-title":"Nuclear targeting of Porphyromonas gingivalis W50 protease in epithelial cells","volume":"70","author":"MA Scragg","year":"2002","journal-title":"Infect Immun"},{"issue":"546","key":"ref58","article-title":"The pseudokinase MLKL activates PAD4-dependent NET formation in necroptotic neutrophils","volume":"11","author":"AA D'Cruz","year":"2018","journal-title":"Science signaling"},{"issue":"6","key":"ref59","doi-asserted-by":"crossref","first-page":"e1002723","DOI":"10.1371\/journal.ppat.1002723","article-title":"Pathogen-mediated proteolysis of the cell death regulator RIPK1 and the host defense modulator RIPK2 in human aortic endothelial cells","volume":"8","author":"AG Madrigal","year":"2012","journal-title":"PLoS Pathog"},{"issue":"6","key":"ref60","doi-asserted-by":"crossref","first-page":"397","DOI":"10.2174\/1389203033487036","article-title":"Gingipains, the major cysteine proteinases and virulence factors of Porphyromonas gingivalis: structure, function and assembly of multidomain protein complexes","volume":"4","author":"J Potempa","year":"2003","journal-title":"Curr Protein Pept Sci"},{"issue":"2","key":"ref61","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1159\/000181145","article-title":"High molecular weight gingipains from Porphyromonas gingivalis induce cytokine responses from human macrophage-like cells via a nonproteolytic mechanism","volume":"1","author":"RE Fitzpatrick","year":"2009","journal-title":"J Innate Immun"},{"key":"ref62","doi-asserted-by":"crossref","first-page":"140","DOI":"10.3389\/fcimb.2017.00140","article-title":"Inactive Gingipains from P. gingivalis Selectively Skews T Cells toward a Th17 Phenotype in an IL-6 Dependent Manner","volume":"7","author":"I Glowczyk","year":"2017","journal-title":"Front Cell Infect Microbiol"},{"issue":"6","key":"ref63","doi-asserted-by":"crossref","first-page":"576","DOI":"10.1159\/000319909","article-title":"Nuclease expression by Staphylococcus aureus facilitates escape from neutrophil extracellular traps","volume":"2","author":"ET Berends","year":"2010","journal-title":"J Innate Immun"},{"issue":"4","key":"ref64","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1016\/j.cub.2006.01.056","article-title":"An endonuclease allows Streptococcus pneumoniae to escape from neutrophil extracellular traps","volume":"16","author":"K Beiter","year":"2006","journal-title":"Curr Biol"},{"issue":"7","key":"ref65","doi-asserted-by":"crossref","first-page":"4319","DOI":"10.4049\/jimmunol.1000893","article-title":"Leishmania donovani promastigotes evade the antimicrobial activity of neutrophil extracellular traps","volume":"185","author":"C Gabriel","year":"2010","journal-title":"J Immunol"},{"issue":"5","key":"ref66","doi-asserted-by":"crossref","first-page":"1073","DOI":"10.1016\/j.peptides.2011.02.003","article-title":"Gingipains produced by Porphyromonas gingivalis ATCC49417 degrade human-beta-defensin 3 and affect peptide's antibacterial activity in vitro","volume":"32","author":"G Maisetta","year":"2011","journal-title":"Peptides"},{"issue":"2\u20133","key":"ref67","first-page":"125","article-title":"Development of a simple chemically defined medium for Porphyromonas gingivalis: requirement for alpha-ketoglutarate","volume":"140","author":"P Milner","year":"1996","journal-title":"FEMS Microbiol Lett"},{"key":"ref68","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1034\/j.1600-0757.2000.2240108.x","article-title":"Role of bacterial proteinases in matrix destruction and modulation of host responses","volume":"24","author":"J Potempa","year":"2000","journal-title":"Periodontol 2000"},{"key":"ref69","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/j.micpath.2015.10.022","article-title":"Bacterial interactions in pathogenic subgingival plaque","volume":"94","author":"HM Ng","year":"2016","journal-title":"Microb Pathog"},{"issue":"5","key":"ref70","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1016\/j.chom.2011.10.006","article-title":"Low-abundance biofilm species orchestrates inflammatory periodontal disease through the commensal microbiota and complement","volume":"10","author":"G Hajishengallis","year":"2011","journal-title":"Cell Host Microbe"},{"issue":"10","key":"ref71","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1038\/nrmicro2873","article-title":"The keystone-pathogen hypothesis","volume":"10","author":"G Hajishengallis","year":"2012","journal-title":"Nature reviews Microbiology"},{"issue":"9","key":"ref72","doi-asserted-by":"crossref","first-page":"816","DOI":"10.1177\/0022034512453589","article-title":"Porphyromonas gingivalis as a potential community activist for disease","volume":"91","author":"RP Darveau","year":"2012","journal-title":"J Dent Res"},{"issue":"5","key":"ref73","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1189\/jlb.71.5.821","article-title":"Neutrophils from MMP-9- or neutrophil elastase-deficient mice show no defect in transendothelial migration under flow in vitro","volume":"71","author":"JR Allport","year":"2002","journal-title":"J Leukoc Biol"},{"issue":"4","key":"ref74","doi-asserted-by":"crossref","first-page":"R137","DOI":"10.1186\/cc11442","article-title":"Depletion of neutrophil extracellular traps in vivo results in hypersusceptibility to polymicrobial sepsis in mice","volume":"16","author":"W Meng","year":"2012","journal-title":"Crit Care"},{"issue":"25","key":"ref75","doi-asserted-by":"crossref","first-page":"17955","DOI":"10.1074\/jbc.274.25.17955","article-title":"Genetic analyses of proteolysis, hemoglobin binding, and hemagglutination of Porphyromonas gingivalis. Construction of mutants with a combination of rgpA, rgpB, kgp, and hagA","volume":"274","author":"Y Shi","year":"1999","journal-title":"J Biol Chem"},{"issue":"1","key":"ref76","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1016\/S0021-9258(17)42365-9","article-title":"Lysine- and arginine-specific proteinases from Porphyromonas gingivalis. Isolation, characterization, and evidence for the existence of complexes with hemagglutinins","volume":"269","author":"R Pike","year":"1994","journal-title":"J Biol Chem"},{"issue":"34","key":"ref77","doi-asserted-by":"crossref","first-page":"21648","DOI":"10.1074\/jbc.273.34.21648","article-title":"Comparative properties of two cysteine proteinases (gingipains R), the products of two related but individual genes of Porphyromonas gingivalis","volume":"273","author":"J Potempa","year":"1998","journal-title":"J Biol Chem"},{"issue":"6","key":"ref78","doi-asserted-by":"crossref","first-page":"063703","DOI":"10.1063\/1.4881683","article-title":"AtomicJ: an open source software for analysis of force curves","volume":"85","author":"P Hermanowicz","year":"2014","journal-title":"The Review of scientific instruments"},{"key":"ref79","doi-asserted-by":"crossref","first-page":"1999","DOI":"10.3389\/fimmu.2017.01999","article-title":"NETQUANT: Automated Quantification of Neutrophil Extracellular Traps","volume":"8","author":"T Mohanty","year":"2017","journal-title":"Front Immunol"},{"key":"ref80","first-page":"413","article-title":"Automatic quantification of in vitro NET formation","volume":"3","author":"V Brinkmann","year":"2012","journal-title":"Front Immunol"}],"updated-by":[{"DOI":"10.1371\/journal.ppat.1007773","type":"new_version","label":"New version","source":"publisher","updated":{"date-parts":[[2019,5,31]],"date-time":"2019-05-31T00:00:00Z","timestamp":1559260800000}}],"container-title":["PLOS Pathogens"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.ppat.1007773","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,9,16]],"date-time":"2023-09-16T19:23:40Z","timestamp":1694892220000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.ppat.1007773"}},"subtitle":[],"editor":[{"given":"Christopher M.","family":"Sassetti","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2019,5,20]]},"references-count":80,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2019,5,20]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.ppat.1007773","relation":{"new_version":[{"id-type":"doi","id":"10.1371\/journal.ppat.1007773","asserted-by":"object"}]},"ISSN":["1553-7374"],"issn-type":[{"value":"1553-7374","type":"electronic"}],"subject":[],"published":{"date-parts":[[2019,5,20]]}}}