Number of the records: 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.
SYSNO ASEP 0345737 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title 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 Author(s) Kotsyfakis, Michalis (BC-A) RID, ORCID
Horká, Helena (BC-A) RID
Salát, Jiří (BC-A) RID, ORCID
Andersen, J. F. (US)Source Title Molecular Microbiology - ISSN 0950-382X
Roč. 77, č. 2 (2010), s. 456-470Number of pages 15 s. Language eng - English Country GB - United Kingdom Keywords INVARIANT CHAIN FRAGMENT ; EGG-WHITE CYSTATIN ; CATHEPSIN-L ; CYSTEINE PROTEINASES ; SIALOSTATIN-L ; ENDOPEPTIDASE Subject RIV EC - Immunology 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) CEZ AV0Z60220518 - PAU-O, BC-A (2005-2011) UT WOS 000279540600014 DOI 10.1111/j.1365-2958.2010.07220.x Annotation We 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. Workplace Biology Centre (since 2006) Contact Dana Hypšová, eje@eje.cz, Tel.: 387 775 214 Year of Publishing 2011
Number of the records: 1