Interpain A, a cysteine proteinase from Prevotella intermedia, inhibits complement by degrading complement factor C3.

Periodontitis is an inflammatory disease of the supporting structures of the teeth caused by, among other pathogens, Prevotella intermedia. Many strains of P. intermedia are resistant to killing by the human complement system, which is present at up to 70% of serum concentration in gingival crevicul...

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Autores principales:	Michal Potempa, Jan Potempa, Tomasz Kantyka, Ky-Anh Nguyen, Katarzyna Wawrzonek, Surya P Manandhar, Katarzyna Popadiak, Kristian Riesbeck, Sigrun Eick, Anna M Blom
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2009
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/03943fbd08b84d9db3dd9420bf82f37d
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spelling	oai:doaj.org-article:03943fbd08b84d9db3dd9420bf82f37d2021-11-25T05:47:14ZInterpain A, a cysteine proteinase from Prevotella intermedia, inhibits complement by degrading complement factor C3.1553-73661553-737410.1371/journal.ppat.1000316https://doaj.org/article/03943fbd08b84d9db3dd9420bf82f37d2009-02-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/19247445/pdf/?tool=EBIhttps://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Periodontitis is an inflammatory disease of the supporting structures of the teeth caused by, among other pathogens, Prevotella intermedia. Many strains of P. intermedia are resistant to killing by the human complement system, which is present at up to 70% of serum concentration in gingival crevicular fluid. Incubation of human serum with recombinant cysteine protease of P. intermedia (interpain A) resulted in a drastic decrease in bactericidal activity of the serum. Furthermore, a clinical strain 59 expressing interpain A was more serum-resistant than another clinical strain 57, which did not express interpain A, as determined by Western blotting. Moreover, in the presence of the cysteine protease inhibitor E64, the killing of strain 59 by human serum was enhanced. Importantly, we found that the majority of P. intermedia strains isolated from chronic and aggressive periodontitis carry and express the interpain A gene. The protective effect of interpain A against serum bactericidal activity was found to be attributable to its ability to inhibit all three complement pathways through the efficient degradation of the alpha-chain of C3 -- the major complement factor common to all three pathways. P. intermedia has been known to co-aggregate with P. gingivalis, which produce gingipains to efficiently degrade complement factors. Here, interpain A was found to have a synergistic effect with gingipains on complement degradation. In addition, interpain A was able to activate the C1 complex in serum, causing deposition of C1q on inert and bacterial surfaces, which may be important at initial stages of infection when local inflammatory reaction may be beneficial for a pathogen. Taken together, the newly characterized interpain A proteinase appears to be an important virulence factor of P. intermedia.Michal PotempaJan PotempaTomasz KantykaKy-Anh NguyenKatarzyna WawrzonekSurya P ManandharKatarzyna PopadiakKristian RiesbeckSigrun EickAnna M BlomPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 5, Iss 2, p e1000316 (2009)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Michal Potempa Jan Potempa Tomasz Kantyka Ky-Anh Nguyen Katarzyna Wawrzonek Surya P Manandhar Katarzyna Popadiak Kristian Riesbeck Sigrun Eick Anna M Blom Interpain A, a cysteine proteinase from Prevotella intermedia, inhibits complement by degrading complement factor C3.
description	Periodontitis is an inflammatory disease of the supporting structures of the teeth caused by, among other pathogens, Prevotella intermedia. Many strains of P. intermedia are resistant to killing by the human complement system, which is present at up to 70% of serum concentration in gingival crevicular fluid. Incubation of human serum with recombinant cysteine protease of P. intermedia (interpain A) resulted in a drastic decrease in bactericidal activity of the serum. Furthermore, a clinical strain 59 expressing interpain A was more serum-resistant than another clinical strain 57, which did not express interpain A, as determined by Western blotting. Moreover, in the presence of the cysteine protease inhibitor E64, the killing of strain 59 by human serum was enhanced. Importantly, we found that the majority of P. intermedia strains isolated from chronic and aggressive periodontitis carry and express the interpain A gene. The protective effect of interpain A against serum bactericidal activity was found to be attributable to its ability to inhibit all three complement pathways through the efficient degradation of the alpha-chain of C3 -- the major complement factor common to all three pathways. P. intermedia has been known to co-aggregate with P. gingivalis, which produce gingipains to efficiently degrade complement factors. Here, interpain A was found to have a synergistic effect with gingipains on complement degradation. In addition, interpain A was able to activate the C1 complex in serum, causing deposition of C1q on inert and bacterial surfaces, which may be important at initial stages of infection when local inflammatory reaction may be beneficial for a pathogen. Taken together, the newly characterized interpain A proteinase appears to be an important virulence factor of P. intermedia.
format	article
author	Michal Potempa Jan Potempa Tomasz Kantyka Ky-Anh Nguyen Katarzyna Wawrzonek Surya P Manandhar Katarzyna Popadiak Kristian Riesbeck Sigrun Eick Anna M Blom
author_facet	Michal Potempa Jan Potempa Tomasz Kantyka Ky-Anh Nguyen Katarzyna Wawrzonek Surya P Manandhar Katarzyna Popadiak Kristian Riesbeck Sigrun Eick Anna M Blom
author_sort	Michal Potempa
title	Interpain A, a cysteine proteinase from Prevotella intermedia, inhibits complement by degrading complement factor C3.
title_short	Interpain A, a cysteine proteinase from Prevotella intermedia, inhibits complement by degrading complement factor C3.
title_full	Interpain A, a cysteine proteinase from Prevotella intermedia, inhibits complement by degrading complement factor C3.
title_fullStr	Interpain A, a cysteine proteinase from Prevotella intermedia, inhibits complement by degrading complement factor C3.
title_full_unstemmed	Interpain A, a cysteine proteinase from Prevotella intermedia, inhibits complement by degrading complement factor C3.
title_sort	interpain a, a cysteine proteinase from prevotella intermedia, inhibits complement by degrading complement factor c3.
publisher	Public Library of Science (PLoS)
publishDate	2009
url	https://doaj.org/article/03943fbd08b84d9db3dd9420bf82f37d
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Interpain A, a cysteine proteinase from Prevotella intermedia, inhibits complement by degrading complement factor C3.

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