Počet záznamů: 1
SmSP2: A serine protease secreted by the blood fluke pathogen Schistosoma mansoni with anti-hemostatic properties
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SYSNO ASEP 0491001 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název SmSP2: A serine protease secreted by the blood fluke pathogen Schistosoma mansoni with anti-hemostatic properties Tvůrce(i) Leontovyč, Adrian (UOCHB-X) ORCID
Ulrychová, Lenka (UOCHB-X) ORCID, RID
O'Donoghue, A.J. (US)
Vondrášek, Jiří (UOCHB-X) RID, ORCID
Marešová, Lucie (UOCHB-X) RID
Hubálek, Martin (UOCHB-X) RID, ORCID
Fajtová, Pavla (UOCHB-X) RID, ORCID
Chanová, M. (CZ)
Jiang, Z. (US)
Craik, C. S. (US)
Caffrey, C. R. (US)
Mareš, Michael (UOCHB-X) RID, ORCID
Dvořák, Jan (UOCHB-X) ORCID
Horn, Martin (UOCHB-X) RID, ORCIDČíslo článku e0006446 Zdroj.dok. PLoS Neglected Tropical Diseases. - : Public Library of Science - ISSN 1935-2735
Roč. 12, č. 4 (2018)Poč.str. 26 s. Jazyk dok. eng - angličtina Země vyd. US - Spojené státy americké Klíč. slova Echinococcus granulosus ; cathepsin B ; molecular characterization Vědní obor RIV CE - Biochemie Obor OECD Biochemistry and molecular biology CEP LD15101 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy LH15040 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy LO1302 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Institucionální podpora UOCHB-X - RVO:61388963 UT WOS 000433487700071 EID SCOPUS 85046346355 DOI 10.1371/journal.pntd.0006446 Anotace Background: Serine proteases are important virulence factors for many pathogens. Recently, we discovered a group of trypsin-like serine proteases with domain organization unique to flatworm parasites and containing a thrombospondin type 1 repeat (TSR-1). These proteases are recognized as antigens during host infection and may prove useful as anthelminthic vaccines, however their molecular characteristics are under-studied. Here, we characterize the structural and proteolytic attributes of serine protease 2 (SmSP2) from Schistosoma mansoni, one of the major species responsible for the tropical infectious disease, schistosomiasis. Methodology/Principal findings: SmSP2 comprises three domains: a histidine stretch, TSR-1 and a serine protease domain. The cleavage specificity of recombinant SmSP2 was determined using positional scanning and multiplex combinatorial libraries and the determinants of specificity were identified with 3D homology models, demonstrating a trypsin-like endopeptidase mode of action. SmSP2 displayed restricted proteolysis on protein substrates. It activated tissue plasminogen activator and plasminogen as key components of the fibrinolytic system, and released the vasoregulatory peptide, kinin, from kininogen. SmSP2 was detected in the surface tegument, esophageal glands and reproductive organs of the adult parasite by immunofluorescence microscopy, and in the excretory/secretory products by immunoblotting. Conclusions/Significance: The data suggest that SmSP2 is secreted, functions at the host-parasite interface and contributes to the survival of the parasite by manipulating host vasodilatation and fibrinolysis. SmSP2 may be, therefore, a potential target for anti-schistosomal therapy. Pracoviště Ústav organické chemie a biochemie Kontakt asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Rok sběru 2019 Elektronická adresa http://journals.plos.org/plosntds/article?id=10.1371/journal.pntd.0006446
Počet záznamů: 1