Počet záznamů: 1  

Trypsin- and Chymotrypsin-Like Serine Proteases in Schistosoma mansoni - 'The Undiscovered Country'

  1. 1. 0429904 - UOCHB-X 2015 RIV US eng J - Článek v odborném periodiku
    Horn, Martin - Fajtová, Pavla - Arreola, L. R. - Ulrychová, Lenka - Bartošová-Sojková, Pavla - Franta, Zdeněk - Protasio, A. V. - Opavský, David - Vondrášek, Jiří - McKerrow, J. H. - Mareš, Michael - Caffrey, C. R. - Dvořák, Jan
    Trypsin- and Chymotrypsin-Like Serine Proteases in Schistosoma mansoni - 'The Undiscovered Country'.
    PLoS Neglected Tropical Diseases. Roč. 8, č. 3 (2014), e2766/1-e2766/13. ISSN 1935-2735
    Grant CEP: GA ČR(CZ) GAP302/11/1481; GA MŠk(CZ) ME10011
    GRANT EU: European Commission(XE) 248642 - SCHISTOSOMA PROTEASE
    Institucionální podpora: RVO:61388963 ; RVO:68378050 ; RVO:60077344
    Klíčová slova: schistosomiasis * blood fluke * serine protease
    Kód oboru RIV: CE - Biochemie; EB - Genetika a molekulární biologie (UMG-J); FN - Epidemiologie, infek. nemoci a klin. imunologie (BC-A)
    Impakt faktor: 4.446, rok: 2014
    http://www.plosntds.org/article/info%3Adoi%2F10.1371%2Fjournal.pntd.0002766

    Schistosomes are blood flukes that live in the blood system and cause chronic and debilitating infection in hundreds of millions of people. Proteolytic enzymes (proteases) produced by the parasite allow it to survive and reproduce. We focused on understanding the repertoire of trypsin- and chymotrypsin-like Schistosoma mansoni serine proteases (SmSPs) using a variety of genomic, bioinformatics, RNA- and protein-based techniques. We identified five SmSPs that are produced at different stages of the parasite's development. Based on bioinformatics and cleavage preferences for small peptide substrates, SmSP1 to SmSP4 are trypsin-like, whereas SmSP5 is chymotrypsin-like. Interestingly, SmSP5 forms part of a ‘missing link’ group of enzymes between the specialized chymotrypsin-like ‘cercarial elastases’ that help the parasite invade human skin and the more typical chymotrypsins and trypsins found in the nature. Our findings form a basis for further exploration of the functions of the individual enzymes, including their possible contributions to influencing host physiology.
    Trvalý link: http://hdl.handle.net/11104/0234956