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Crystal structure and functional characterization of an immunomodulatory salivary cystatin from the soft tick Ornithodoros moubata

SYSNO ASEP	0345741
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	Crystal structure and functional characterization of an immunomodulatory salivary cystatin from the soft tick Ornithodoros moubata
Author(s)	Salát, Jiří (BC-A)_{RID, ORCID} Paesen, G.C. (GB) Řezáčová, Pavlína (UOCHB-X)_{RID, ORCID} Kotsyfakis, Michalis (BC-A)_{RID, ORCID} Kovářová, Zuzana (UOCHB-X)_{RID, ORCID} Šanda, Miloslav (UOCHB-X) Majtán, J. (GB) Grunclová, Lenka (BC-A) Horká, Helena (BC-A)_RID Andersen, J. F. (US) Brynda, Jiří (UMG-J)_RID Horn, Martin (UOCHB-X)_{RID, ORCID} Nunn, M. A. (GB) Kopáček, Petr (BC-A)_{RID, ORCID} Kopecký, Jan (BC-A)_RID Mareš, Michael (UOCHB-X)_{RID, ORCID}
Source Title	Biochemical Journal. - : Portland Press - ISSN 0264-6021 Roč. 429, č. 1 (2010), s. 103-112
Number of pages	10 s.
Language	eng - English
Country	GB - United Kingdom
Keywords	cathepsin ; cystatin ; Ornithodoros moubata ; parasite ; peptidase inhibitor
Subject RIV	EB - Genetics ; Molecular Biology
R&D Projects	KJB500960702 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR)
	IAA600960811 GA AV ČR - Academy of Sciences of the Czech Republic (AV ČR)
	GAP207/10/2183 GA ČR - Czech Science Foundation (CSF)
	LC06009 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
CEZ	AV0Z60220518 - PAU-O, BC-A (2005-2011)
	AV0Z40550506 - UOCHB-X (2005-2011)
	AV0Z50520514 - UMG-J (2005-2011)
UT WOS	000279418500011
DOI	10.1042/BJ20100280
Annotation	Using proteomic analysis, the cystatin OmC2 was demonstrated in the saliva of the soft tick Ornithodoros moubata. A structural, biochemical and biological characterization of this peptidase inhibitor was undertaken in the present study. Recombinant OmC2 was screened against a panel of physiologically relevant peptidases and was found to be an effective broad-specificity inhibitor of cysteine cathepsins, including endopeptidases (cathepsins L and S) and exopeptidases (cathepsins B, C and H). The crystal structure of OmC2 was determined at a resolution of 2.45 angstrom (1 angstrom = 0.1 nm) and was used to describe the structure inhibitory activity relationship. The biological impact of OmC2 was demonstrated both in vitro and in vivo. OmC2 affected the function of antigen-presenting mouse dendritic cells by reducing the production of the pro-inflammatory cytokines tumour necrosis factor alpha and interleukin-12, and proliferation of antigen-specific CD4(+) T-cells.
Workplace	Biology Centre (since 2006)
Contact	Dana Hypšová, eje@eje.cz, Tel.: 387 775 214
Year of Publishing	2011

Number of the records: 1