Background: Serpins are a superfamily of serine peptidase inhibitors that participate in the regulation of many physiological and cell peptidase-mediated processes in all organisms (e.g. in blood clotting, complement activation, fibrinolysis, inflammation, and programmed cell death). It was postulated that in the blood-feeding members of the monogenean family Diplozoidae, serpins could play an important role in the prevention of thrombus formation, activation of complement, inflammation in the host, and/or in the endogenous regulation of protein degradation.
Results: In silico analysis showed that the DNA and primary protein structures of serpin from Eudiplozoon nipponicum (EnSerp1) are similar to other members of the serpin superfamily. The inhibitory potential of EnSerp1 on four physiologically-relevant serine peptidases (trypsin, factor Xa, kallikrein, and plasmin) was demonstrated and its presence in the worm’s excretory-secretory products (ESPs) was confirmed.
Conclusion: EnSerp1 influences the activity of peptidases that play a role in blood coagulation, fibrinolysis, and complement activation. This inhibitory potential, together with the serpin’s presence in ESPs, suggests that it is likely involved in host-parasite interactions and could be one of the molecules involved in the control of feeding and prevention of inflammatory responses.
The ever-increasing number of Lyme borreliosis patients led us to consider more effective procedures for disease prevention. The aim of our study was to monitor the annual activity and infectivity of Ixodes ricinus ticks in the Pisárky region, City of Brno, CR, and to test the responses of the locally-captured ticks to selected repellents. The result of regular one-hourper-week monitoring in 2011 was the collection of ticks that directly reflected the highest number of Lyme disease patients (4,835) detected throughout the period of recording in the Czech Republic. The ticks were examined for spirochaetes by dark field microscopy. The positive samples were identified by PCR analysis, confirming that 76% of these were infected with Borrelia burgdorferi sensu lato. Ticks were most abundant in May and June, with August having the highest risk for spirochaetal infection. Tick activity was statistically correlated with temperature. The moving-object-bioassay was used to study repellent efficiency on the Ixodes ricinus nymphs captured in the above-mentioned suburban park. Five selected commercial repellents based on DEET (N, N-diethyl-3-methylbenzamide) showed statistically different effects on the non-repellent control group. Journal of Vector Ecology 38 (2): 295-300. 2013.
Ticks represent the primary vectors of several serious diseases, including the Lyme disease caused by Borrelia burgdorferi sensu lato (Bbsl). In this study two dominant ectoparasitic groups of arthropods (Mesostigmata, Siphonaptera) were investigated for the presence of borrelian DNA in order to determine their potential role of vectors (or carriers) of this bacterium. All individuals (235) were collected from wild-living rodents obtained in three localities in the Czech Republic (Bažantula, Baba and Křižovice). The majority of parasites were members of the families Parasitidae and Dermanyssidae (Mesostigmata) and families Hystrichopsyllidae and Ceratophyllidae (Siphonaptera). The rodent host species was almost exclusively the yellow-necked mouse (Apodemus flavicollis). Bbsl was detected by the PCR method in the following ectoparasite species: Euryparasitus emarginatus (1), Eulaelaps stabularis (1), Haemogamassus nidi (1), Laelaps agilis (5), Myonyssus gigas (1) (Mesostigmata) and Ctenophthalmus agyrtes (1), C. solutus (3) (Siphonaptera).
In current work, we used recombinant OspC protein derived from B. afzelii strain BRZ31 in the native homodimeric fold for mice immunization and following selection process to produce three mouse monoclonal antibodies able to bind to variable parts of up to five different OspC proteins. Applying the combination of mass spectrometry assisted epitope mapping and affinity based theoretical prediction we have localized regions responsible for antigen-antibody interactions and approximate epitopes' amino acid composition. Two mAbs (3F4 and 2A9) binds to linear epitopes located in previously described immunogenic regions in the exposed part of OspC protein. The third mAb (2D1) recognises highly conserved discontinuous epitope close to the ligand binding domain 1.
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