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Tannerella forsythia: regulation of intra- and extracellular proteolytic activity in pathogenicity mechanism.

2011/03/N/NZ1/00586

Keywords:

periodontitis Tannerella forsythia serpins proteases inhibition of serine proteases

Descriptors:

  • NZ1_2: Biochemistry
  • NZ1_1: Molecular biology

Panel:

NZ1 - Molecular biology, structural biology, biotechnology: molecular biology, structural biology, biotechnology

Host institution :

Uniwersytet Jagielloński, Wydział Biochemii, Biofizyki i Biotechnologii

woj. małopolskie

Other projects carried out by the institution 

Principal investigator (from the host institution):

Mirosław Książek 

Number of co-investigators in the project: 2

Call: PRELUDIUM 2 - announced on 2011-09-15

Amount awarded: 192 400 PLN

Project start date (Y-m-d): 2012-09-17

Project end date (Y-m-d): 2014-09-16

Project duration:: 24 months (the same as in the proposal)

Project status: Project settled

Information in the final report

  • Publication in academic press/journals (4)
  1. Inhibition of gingipains by their profragments as the mechanism protecting Porphyromonas gingivalis against premature activation of secreted proteases.
    Authors:
    Veillard F, Sztukowska M, Mizgalska D, Ksiazek M, Houston J, Potempa B, Enghild JJ, Thogersen IB, Gomis-Rüth FX, Nguyen KA, Potempa J.
    Academic press:
    BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS (rok: 2013, tom: 1830, strony: 4218-4228), Wydawca: Elsevier
    Status:
    Published
    DOI:
    10.1016/j.bbagen.2013.04.005 - link to the publication
  2. Mirolase, a novel subtilisin-like serine protease from the periodontopathogen Tannerella forsythia.
    Authors:
    Ksiazek M, Karim AY, Bryzek D, Enghild JJ, Thøgersen IB, Koziel J, Potempa J
    Academic press:
    Biological Chemistry (rok: 2015, tom: 396, strony: 261-75), Wydawca: De Gruyter
    Status:
    Published
    DOI:
    10.1515/hsz-2014-0256 - link to the publication
  3. Miropin, a novel bacterial serpin from the periodontopathogen Tannerella forsythia, inhibits a broad range of proteases by using different peptide bonds within the reactive center loop.
    Authors:
    Ksiazek M, Mizgalska D, Enghild JJ, Scavenius C, Thogersen IB, Potempa J
    Academic press:
    The Journal of Biological Chemistry (rok: 2015, tom: 290, strony: 658-70), Wydawca: American Society of Biochemistry and Molecular Biology
    Status:
    Published
    DOI:
    10.1074/jbc.M114.601716 - link to the publication
  4. Structure of the catalytic domain of the Tannerella forsythia matrix metallopeptidase karilysin in complex with a tetrapeptidic inhibitor
    Authors:
    Guevara T, Ksiazek M, Skottrup PD, Cerdà-Costa N, Trillo-Muyo S, de Diego I, Riise E, Potempa J, Gomis-Rüth FX
    Academic press:
    Acta Crystallogr Sect F Struct Biol Cryst Commun. (rok: 2013, tom: 69, strony: 472-6), Wydawca: International Union of Crystallography
    Status:
    Published
    DOI:
    10.1107/S1744309113007392 - link to the publication

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