Počet záznamů: 1  

The crystal structures of two salivary cystatins from the tick Ixodes scapularis and the effect of these inhibitors on the establishment of Borrelia burgdorferi infection in a murine model

  1. 1.
    SYSNO ASEP0345737
    Druh ASEPJ - Článek v odborném periodiku
    Zařazení RIVJ - Článek v odborném periodiku
    Poddruh JČlánek ve WOS
    NázevThe crystal structures of two salivary cystatins from the tick Ixodes scapularis and the effect of these inhibitors on the establishment of Borrelia burgdorferi infection in a murine model
    Tvůrce(i) Kotsyfakis, Michalis (BC-A) RID, ORCID
    Horká, Helena (BC-A) RID
    Salát, Jiří (BC-A) RID, ORCID
    Andersen, J. F. (US)
    Zdroj.dok.Molecular Microbiology - ISSN 0950-382X
    Roč. 77, č. 2 (2010), s. 456-470
    Poč.str.15 s.
    Jazyk dok.eng - angličtina
    Země vyd.GB - Velká Británie
    Klíč. slovaINVARIANT CHAIN FRAGMENT ; EGG-WHITE CYSTATIN ; CATHEPSIN-L ; CYSTEINE PROTEINASES ; SIALOSTATIN-L ; ENDOPEPTIDASE
    Vědní obor RIVEC - Imunologie
    CEPKJB500960702 GA AV ČR - Akademie věd
    IAA600960811 GA AV ČR - Akademie věd
    CEZAV0Z60220518 - PAU-O, BC-A (2005-2011)
    UT WOS000279540600014
    DOI10.1111/j.1365-2958.2010.07220.x
    AnotaceWe have previously demonstrated that two salivary cysteine protease inhibitors from the Borrelia burgdorferi (Lyme disease) vector Ixodes scapularis play an important role in tick biology. Here we show that sialostatin L2 - but not sialostatin L - facilitates the growth of B. burgdorferi in murine skin. To examine the structural basis underlying these differential effects of the two sialostatins, we have determined the crystal structures of both sialostatin L and L2. This is the first structural analysis of cystatins from an invertebrate source. Sialostatin L2 crystallizes as a monomer with an 'unusual' conformation of the N-terminus, while sialostatin L crystallizes as a domain-swapped dimer with an N-terminal conformation similar to other cystatins. Deletion of the 'unusual' N-terminal five residues of sialostatin L2 results in marked changes in its selectivity, suggesting that this region is a particularly important determinant of the biochemical activity of sialostatin L2.
    PracovištěBiologické centrum (od r. 2006)
    KontaktDana Hypšová, eje@eje.cz, Tel.: 387 775 214
    Rok sběru2011
Počet záznamů: 1  

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