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Přítomnost nízkomolekulárních imunomodulátorů ve slinách klíštěte \kur{Ixodes ricinus}
HAUSEROVÁ, Simona
Ticks use proteinaceous molecules contained in their saliva to suppress immune response of the host to complete their succesful feeding. In some ticks (e.g. Rhipicephalus sanguineus) presence of non-proteinaceous molecules was discovered. The aim of this work was to determine the amount of these molecules in the saliva of Ixodes ricinus tick. Namely, prostaglandin E2 and adenosine were analyzed. The second aim of this work was to evaluate the role of both low molecular weight components (or at least one of them) in the suppression of TNF-alfa cytokine production in suitable cells by ticks saliva.
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Determination of N-glycome of the tick \kur{Ixodes ricinus} and \kur{Dermacentor marginatus}; Analysis of N-glycans in tick tissues and their comparison
ŠIMONOVÁ, Zuzana
Glycosylation in vertebrates has a main role in many important processes such as cell transport, protein folding, secretion of proteins etc. What function has glycosylation in arthropods, for example in ticks, is rarely studied. This work was focused on analysis of N-glycans in tick tissues, namely in Ixodes ricinus and Dermacentor marginatus. High-mannose glycans as well as complex glycans with or without core-fucosylation were identified in this study.Furthermore several sialylated glycans were present in the studied samples. Sialic acid is found in arthropods rarely and this is the first study which directly proves its presence in ticks using mass spectrometry.
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Analyses of glycoproteins from the salivary glands of the tick \kur{Ixodes ricinus}
BUČINSKÁ, Lenka
I characterized several potential glycoproteins in salivary gland extracts from unfed and partially fed females of ticks Ixodes ricinus using enzyme deglycosylation and lectin labeling. Affinity-based (chromatografic) analysis was applied for isolations of glycoproteins with specificity for GNA (mannose), HPA (N-acetylgalactosamine) and MAA II (sialic acid) lectins. GNA specific 120 kDa glycoprotein was isolated from partially fed females and is modified with N-linked glycans containing {$\alpha$}1,3-mannose. Mass spectrometry analyses confirmed the presence carboxypeptidase M in elution fraction gain with GNA affinity chromatography. GNA specific proteins were purified from unfed female salivary gland extracts. MS analyses identified them as proteins similar to arylsulfatase B and cytoskeletal Sojo protein. Proteins (85 and 56 kDa) isolated with HPA affinity chromatography were characterized as Trappin 12, which is a host protein. MAA II lectin was used for labelling and isolation of 100 kDa protein. N-terminal sequence of the MAA II specific protein predicted similarity with a host protein, Siglec 1. Fucose in salivary gland extract was detected with the labelling of AAA, AAL, UEA I and LTL lectins. Results showed that salivary gland extracts contain {$\alpha$}1,2-; {$\alpha$}1,3- and {$\alpha$}1,6- N-linked fucose and O-linked fucose probably as well. GNA specific proteins were detected in partially fed salivary glands acini type II and III using electron transmission microscopy. Fucose was detected on gut and salivary gland structures using fucose-specific lectin AAL.
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