Vector-borne diseases constitute 17% of all infectious diseases in the world; among the blood-feeding arthropods, ticks transmit the highest number of pathogens. Understanding the interactions between the tick vector, the mammalian host and the pathogens circulating between them is the basis for the successful development of vaccines against ticks or the tick-transmitted pathogens as well as for the development of specific treatments against tick-borne infections. A lot of effort has been put into transcriptomic and proteomic analyses; however, the protein-carbohydrate interactions and the overall glycobiology of ticks and tick-borne pathogens has not been given the importance or priority deserved. Novel (bio)analytical techniques and their availability have immensely increased the possibilities in glycobiology research and thus novel information in the glycobiology of ticks and tick-borne pathogens is being generated at a faster pace each year. This review brings a comprehensive summary of the knowledge on both the glycosylated proteins and the glycan-binding proteins of the ticks as well as the tick-transmitted pathogens, with emphasis on the interactions allowing the infection of both the ticks and the hosts by various bacteria and tick-borne encephalitis virus.

• Klíčová slova
• Anaplasma, Borrelia, Carbohydrate-binding, Glycan, Glycobiology, Host, Lectin, Pathogen, TBEV, Tick,
• MeSH
• Anaplasma patogenita   MeSH
• Borrelia patogenita   MeSH
• glykomika metody   MeSH
• glykosylace MeSH
• interakce hostitele a patogenu fyziologie   MeSH
• klíště mikrobiologie   fyziologie   virologie   MeSH
• lektiny metabolismus   MeSH
• nemoci přenášené klíšťaty patofyziologie   MeSH
• polysacharidy metabolismus   MeSH
• proteomika MeSH
• sacharidy fyziologie   MeSH
• viry klíšťové encefalitidy patogenita   MeSH
• zvířata MeSH
• Check Tag
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• přehledy MeSH
• Názvy látek
• lektiny MeSH
• polysacharidy MeSH
• sacharidy MeSH

The aim of the study is co-localization of N-glycans with fucose attached to N-acetylglucosamine in α1,3 linkage, that belong to immunogenic carbohydrate epitopes in humans, and N-glycans with α1,6-core fucose typical for mammalian type of N-linked glycosylation. Both glycan epitopes were labelled in cryosections of salivary glands isolated from the tick Ixodes ricinus. Salivary glands secrete during feeding many bioactive molecules and influence both successful feeding and transmission of tick-borne pathogens. For accurate and reliable localization of labelled glycans in both fluorescence and scanning electron microscopes, we used carbon imprints of finder or indexed EM grids on glass slides. We discuss if the topographical images can provide information about labelled structures, the working setting of the field-emission scanning electron microscope and the influence of the detector selection (a below-the-lens Autrata improved YAG detector of back-scattered electrons; in-lens and conventional Everhart-Thornley detectors of secondary electrons) on the imaging of gold nanoparticles, quantum dots and osmium-stained membranes.

• MeSH
• barvení a značení metody   MeSH
• elektronová kryomikroskopie přístrojové vybavení   metody   MeSH
• fluorescenční mikroskopie přístrojové vybavení   metody   MeSH
• klíště * metabolismus   ultrastruktura   MeSH
• mikroskopie elektronová rastrovací přístrojové vybavení   metody   MeSH
• proteiny členovců metabolismus   MeSH
• proteoglykany metabolismus   MeSH
• sklo MeSH
• slinné proteiny a peptidy metabolismus   MeSH
• slinné žlázy * metabolismus   ultrastruktura   MeSH
• uhlík MeSH
• zvířata MeSH
• Check Tag
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• proteiny členovců MeSH
• proteoglykany MeSH
• slinné proteiny a peptidy MeSH
• uhlík MeSH

BACKGROUND: Fibrinogen-related proteins with lectin activity are believed to be part of the tick innate immune system. Several fibrinogen-related proteins have been described and characterised mainly on the basis of their cDNA sequences while direct biochemical evidence is missing. One of them, the haemolymph lectin Dorin M from the tick Ornithodoros moubata was isolated and characterised in more depth. RESULTS: Several fibrinogen-related proteins were detected in the haemolymph of ixodid ticks Dermacentor marginatus, Rhipicephalus appendiculatus, R. pulchellus, and R. sanguineus. These proteins were recognised by sera directed against the tick lectin Dorin M and the haemagglutination activity of the ticks R. appendiculatus and D. marginatus. Cross-reactivity of the identified proteins with antibodies against the fibrinogen domain of the human ficolin was also shown. The carbohydrate-binding ability of tick haemolymph was confirmed by haemagglutination activity assays, and this activity was shown to be inhibited by neuraminic acid and sialylated glycoproteins as well as by N-acetylated hexosamines. The fibrinogen-related proteins were shown to be glycosylated and they were localised in salivary glands, midguts, and haemocytes of D. marginatus. Hemelipoglycoprotein was also recognised by sera directed against the fibrinogen-related proteins in all three Rhipicephalus species as well as in D. marginatus. However, this protein does not contain the fibrinogen domain and thus, the binding possibly results from the structure similarity between hemelipoglycoprotein and the fibrinogen domain. CONCLUSIONS: The presence of fibrinogen-related proteins was shown in the haemolymph of four tick species in high abundance. Reactivity of antibodies directed against ficolin or fibrinogen-related proteins with proteins which do not contain the fibrinogen domain points out the importance of sequence analysis of the identified proteins in further studies. Previously observed expression of fibrinogen-related proteins in haemocytes together with the results of this study suggest involvement of fibrinogen-related proteins in tick immunity processes. Thus, they have potential as targets for anti-tick vaccines and as antimicrobial proteins in pharmacology. Research on fibrinogen-related proteins could reveal further details of tick innate immunity processes.

• MeSH
• anatomické struktury zvířat chemie   MeSH
• Dermacentor chemie   MeSH
• fibrinogen imunologie   MeSH
• fikoliny MeSH
• glykoproteiny imunologie   metabolismus   MeSH
• hemaglutininy imunologie   metabolismus   MeSH
• hmyzí proteiny imunologie   metabolismus   MeSH
• lektiny imunologie   metabolismus   MeSH
• lidé MeSH
• metabolismus sacharidů MeSH
• Ornithodoros chemie   MeSH
• protilátky imunologie   MeSH
• Rhipicephalus chemie   MeSH
• vazba proteinů MeSH
• zkřížené reakce MeSH
• zvířata MeSH
• Check Tag
• lidé MeSH
• ženské pohlaví MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• fibrinogen MeSH
• glykoproteiny MeSH
• hemaglutininy MeSH
• hmyzí proteiny MeSH
• lektiny MeSH
• protilátky MeSH

BACKGROUND: Tick carrier proteins are able to bind, transport, and store host-blood heme, and thus they function also as antioxidants. Nevertheless, the role of carrier proteins in ticks is not fully understood. Some of them are found also in tick males which do not feed on hosts to such an extent such as females (there are differences in male feeding in different tick species) and thus they are not dealing with such an excess of heme; some of the carrier proteins were found in salivary glands where the processing of blood and thus release of heme does not occur. Besides, the carrier proteins bind relatively low amounts of heme (in one case only two molecules of heme per protein) compared to their sizes (above 200 kDa). The main aim of this study is the biochemical characterization of a carrier protein from the ornate sheep tick Dermacentor marginatus, hemelipoglycoprotein, with emphasis on its size in native conditions, its glycosylation and identification of its modifying glycans, and examining its carbohydrate-binding specificity. RESULTS: Hemelipoglycoprotein from D. marginatus plasma was purified in native state by immunoprecipitation and denatured using electroelution from SDS-PAGE separated plasma. The protein (290 kDa) contains two subunits with molecular weights 100 and 95 kDa. It is glycosylated by high-mannose and complex N-glycans HexNAc(2)Hex(9), HexNAc(2)Hex(10), HexNAc(4)Hex(7), and HexNAc(4)Hex(8). The purified protein is able to agglutinate red blood cells and has galactose- and mannose-binding specificity. The protein is recognized by antibodies directed against plasma proteins with hemagglutination activity and against fibrinogen-related lectin Dorin M from the tick Ornithodoros moubata. It forms high-molecular weight complexes with putative fibrinogen-related proteins and other unknown proteins under native conditions in tick plasma. Feeding does not increase its amounts in male plasma. The hemelipoglycoprotein was detected also in hemocytes, salivary glands, and gut. In salivary glands, the protein was present in both glycosylated and nonglycosylated forms. CONCLUSION: A 290 kDa hemelipoglycoprotein from the tick Dermacentor marginatus, was characterized. The protein has two subunits with 95 and 100 kDa, and bears high-mannose and complex N-linked glycans. In hemolymph, it is present in complexes with putative fibrinogen-related proteins. This, together with its carbohydrate-binding activity, suggests its possible involvement in tick innate immunity. In fed female salivary glands, it was found also in a form corresponding to the deglycosylated protein.

• MeSH
• Dermacentor chemie   metabolismus   MeSH
• elektroforéza v polyakrylamidovém gelu MeSH
• glykoproteiny chemie   izolace a purifikace   metabolismus   MeSH
• glykosylace MeSH
• hemaglutininy chemie   izolace a purifikace   metabolismus   MeSH
• hemoproteiny chemie   izolace a purifikace   metabolismus   MeSH
• imunoprecipitace MeSH
• lipoproteiny chemie   izolace a purifikace   metabolismus   MeSH
• metabolismus sacharidů MeSH
• molekulová hmotnost MeSH
• Ornithodoros imunologie   MeSH
• ovce MeSH
• podjednotky proteinů chemie   izolace a purifikace   metabolismus   MeSH
• protilátky imunologie   MeSH
• transportní proteiny chemie   izolace a purifikace   metabolismus   MeSH
• vazba proteinů MeSH
• zkřížené reakce MeSH
• zvířata MeSH
• Check Tag
• mužské pohlaví MeSH
• ženské pohlaví MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• glykoproteiny MeSH
• hemaglutininy MeSH
• hemoproteiny MeSH
• lipoproteiny MeSH
• podjednotky proteinů MeSH
• protilátky MeSH
• transportní proteiny MeSH