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

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About: Crystal structure and functional characterization of an immunomodulatory salivary cystatin from the soft tick Ornithodoros moubata Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://dx.doi.org/10.1042/BJ20100280
Description	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. 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. (en)
Title	Crystal structure and functional characterization of an immunomodulatory salivary cystatin from the soft tick Ornithodoros moubata Crystal structure and functional characterization of an immunomodulatory salivary cystatin from the soft tick Ornithodoros moubata (en)
skos:prefLabel	Crystal structure and functional characterization of an immunomodulatory salivary cystatin from the soft tick Ornithodoros moubata Crystal structure and functional characterization of an immunomodulatory salivary cystatin from the soft tick Ornithodoros moubata (en)
skos:notation	RIV/00216208:11310/10:10109230!RIV12-MSM-11310___
http://linked.open...avai/riv/aktivita	P S Z
http://linked.open...avai/riv/aktivity	P(GAP207/10/2183), P(IAA600960811), P(KJB500960702), P(LC06009), S, Z(AV0Z40550506), Z(AV0Z50520514), Z(AV0Z60220518)
http://linked.open...iv/cisloPeriodika	Part 1
http://linked.open...vai/riv/dodaniDat	2012
http://linked.open...aciTvurceVysledku	Kovářová, Zuzana
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Karlova v Praze / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	252440
http://linked.open...ai/riv/idVysledku	RIV/00216208:11310/10:10109230
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	peptidase inhibitor; parasite; Ornithodoros moubata; cystatin; cathepsin (en)
http://linked.open.../riv/klicoveSlovo	Ornithodoros moubata cathepsin parasite cystatin peptidase inhibitor
http://linked.open...odStatuVydavatele	GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV	[7C5C23A1F7D2]
http://linked.open...i/riv/nazevZdroje	Biochemical Journal
http://linked.open...in/vavai/riv/obor	EB
http://linked.open...ichTvurcuVysledku	1 (xsd:int)
http://linked.open...cetTvurcuVysledku	16 (xsd:int)
http://linked.open...vavai/riv/projekt	Structural proteomics of proteolytic systems in ticks Identification of tick salivary molecules facilitating transmission of Borrelia burgdorferi using RNA interference Centre for molecular ecology of vectors and pathogens IMMUNOMODULATORY EFFECTS OF TICK CYSTATINS
http://linked.open...UplatneniVysledku	2010
http://linked.open...v/svazekPeriodika	429
http://linked.open...iv/tvurceVysledku	Brynda, Jiří Horn, Martin Kotsyfakis, Michalis Kopecký, Jan Kopáček, Petr Kovářová, Zuzana Mareš, Michael Salát, Jiří Řezáčová, Pavlína Šanda, Miloslav Grunclová, Lenka Andersen, John F. Horká, Helena Majtán, Juraj Nunn, Miles A. Paesen, Guido C.
http://linked.open...ain/vavai/riv/wos	000279418500011
http://linked.open...n/vavai/riv/zamer	Regulace biologických procesů: Chemické modulátory vybraných systémů významných pro medicínu a zemědělství Molekulárně genetické a buněčné základy klíčových biologických procesů: genová exprese, onkogeneze, replikace virů, imunita a vývoj organismů Parazitismus a parazito-hostitelské vztahy na organismální, buněčné a molekulové úrovni
issn	0264-6021
number of pages	10 (xsd:int)
http://bibframe.org/vocab/doi	10.1042/BJ20100280
http://localhost/t...ganizacniJednotka	11310

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