Hemelipoglycoprotein from the ornate sheep tick, Dermacentor marginatus: structural and functional characterization

0359405 - BC 2012 RIV GB eng J - Článek v odborném periodiku
Dupejová, J. - Štěrba, Ján - Vancová, Marie - Grubhoffer, Libor
Hemelipoglycoprotein from the ornate sheep tick, Dermacentor marginatus: structural and functional characterization.
Parasites & Vectors. Roč. 4, January (2011), s. 4. ISSN 1756-3305. E-ISSN 1756-3305
Grant CEP: GA MŠMT(CZ) LC06009; GA AV ČR KJB600960906
Výzkumný záměr: CEZ:AV0Z60220518
Klíčová slova: ORNITHODOROS PARKERI * BOOPHILUS MICROPLUS * MASS-SPECTROMETRY * CATTLE TICK * SOFT TICK * DORIN M * PROTEINS * HEMOLYMPH * VITELLOGENIN * LIPOPROTEIN
Kód oboru RIV: EA - Morfologické obory a cytologie
Impakt faktor: 2.937, rok: 2011

Results: Hemelipoglycoprotein from sheep tick Dermacentor 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. 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. 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.
Trvalý link: http://hdl.handle.net/11104/0197202