Charakterizace nových cysteinových proteáz a jejich inhibitorů u hematofágních klíšťat a alergenních roztočů

Orsághová, Katarína

Proteolytic systems play a crucial role in medically relevant arthropods in processes such as host-parasite interactions and the development of allergic hypersensitivity. This dissertation focuses on cathepsin proteases and their inhibitors in blood-feeding ticks and allergenic mites, exploring their function, structure, and biomedical relevance. The following novel molecules were investigated. Thyropin IrThy from the saliva of the hard tick Ixodes ricinus was recombinantly produced and shown to be a highly selective inhibitor of cathepsins K, L, and V. It was structurally characterized by NMR, as the first parasite thyropin, explaining its narrow inhibitory profile. The obtained data suggest a role for IrThy in the early stages of hematophagy. Proteolytic profiling of the allergenic mites Dermatophagoides farinae and Acarus siro identified two novel cathepsin-type cysteine proteases, DfCB and AsCC, which are excreted and contaminate the environment. Enzymatic and proteomic analyses demonstrated that they are distinct from previously known groups of mite protease allergens and may contribute to allergic sensitization. An activity assay for their specific detection was developed. Recombinant DfCB, a cathepsin B-like protease, was functionally characterized, revealing carboxytripeptidase activity...

guest :: login Digital Repository
		Search		Submit		Help		About