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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F11%3A00359405" target="_blank" >RIV/60077344:_____/11:00359405 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60076658:12310/11:43876871

Výsledek na webu

<a href="http://dx.doi.org/10.1186/1756-3305-4-4" target="_blank" >http://dx.doi.org/10.1186/1756-3305-4-4</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1186/1756-3305-4-4" target="_blank" >10.1186/1756-3305-4-4</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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 molecularweights 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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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 molecularweights 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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EA - Morfologické obory a cytologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2011

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Parasites Vectors

ISSN

1756-3305

e-ISSN

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Svazek periodika

4

Číslo periodika v rámci svazku

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Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

10

Strana od-do

4

Kód UT WoS článku

000286388600001

EID výsledku v databázi Scopus

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