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Salivary Tick Cystatin OmC2 Targets Lysosomal Cathepsins S and C in Human Dendritic Cells
T. Zavašnik-Bergant, R. Vidmar, A. Sekirnik, M. Fonović, J. Salát, L. Grunclová, P. Kopáček, B. Turk,
Jazyk angličtina Země Švýcarsko
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Directory of Open Access Journals
od 2011
Free Medical Journals
od 2011
PubMed Central
od 2011
Europe PubMed Central
od 2011
Open Access Digital Library
od 2011-01-01
Open Access Digital Library
od 2011-01-01
ROAD: Directory of Open Access Scholarly Resources
od 2011
PubMed
28713775
DOI
10.3389/fcimb.2017.00288
Knihovny.cz E-zdroje
- MeSH
- antigeny CD86 MeSH
- antigeny diferenciační B-lymfocytární MeSH
- buněčné linie MeSH
- cystatiny metabolismus MeSH
- dendritické buňky imunologie metabolismus MeSH
- epoxidové sloučeniny imunologie metabolismus MeSH
- geny MHC třídy II imunologie MeSH
- kathepsin C metabolismus MeSH
- kathepsiny chemie imunologie metabolismus MeSH
- klíšťata enzymologie MeSH
- lidé MeSH
- lyzozomy enzymologie MeSH
- MHC antigeny II. třídy MeSH
- Ornithodoros enzymologie MeSH
- rekombinantní proteiny MeSH
- sliny enzymologie MeSH
- tyrosin analogy a deriváty imunologie metabolismus MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
To ensure successful feeding tick saliva contains a number of inhibitory proteins that interfere with the host immune response and help to create a permissive environment for pathogen transmission. Among the potential targets of the salivary cystatins are two host cysteine proteases, cathepsin S, which is essential for antigen- and invariant chain-processing, and cathepsin C (dipeptidyl peptidase 1, DPP1), which plays a critical role in processing and activation of the granule serine proteases. Here, the effect of salivary cystatin OmC2 fromOrnithodoros moubatawas studied using differentiated MUTZ-3 cells as a model of immature dendritic cells of the host skin. Following internalization, cystatin OmC2 was initially found to inhibit the activity of several cysteine cathepsins, as indicated by the decreased rates of degradation of fluorogenic peptide substrates. To identify targets, affinity chromatography was used to isolate His-tagged cystatin OmC2 together with the bound proteins from MUTZ-3 cells. Cathepsins S and C were identified in these complexes by mass spectrometry and confirmed by immunoblotting. Furthermore, reduced increase in the surface expression of MHC II and CD86, which are associated with the maturation of dendritic cells, was observed. In contrast, human inhibitor cystatin C, which is normally expressed and secreted by dendritic cells, did not affect the expression of CD86. It is proposed that internalization of salivary cystatin OmC2 by the host dendritic cells targets cathepsins S and C, thereby affecting their maturation.
Department of Biochemistry Molecular and Structural Biology Jožef Stefan InstituteLjubljana Slovenia
Institute of Parasitology Biology Centre of the Czech Academy of SciencesČeské Budějovice Czechia
Citace poskytuje Crossref.org
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