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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,
Language English Country Switzerland
Document type Journal Article, Research Support, Non-U.S. Gov't
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- MeSH
- B7-2 Antigen MeSH
- Antigens, Differentiation, B-Lymphocyte MeSH
- Cell Line MeSH
- Cystatins metabolism MeSH
- Dendritic Cells immunology metabolism MeSH
- Epoxy Compounds immunology metabolism MeSH
- Genes, MHC Class II immunology MeSH
- Cathepsin C metabolism MeSH
- Cathepsins chemistry immunology metabolism MeSH
- Ticks enzymology MeSH
- Humans MeSH
- Lysosomes enzymology MeSH
- Histocompatibility Antigens Class II MeSH
- Ornithodoros enzymology MeSH
- Recombinant Proteins MeSH
- Saliva enzymology MeSH
- Tyrosine analogs & derivatives immunology metabolism MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't 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
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