The majority of sialylated glycoproteins in adult Ixodes ricinus ticks originate in the host, not the tick
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
24680516
DOI
10.1016/j.carres.2014.02.017
PII: S0008-6215(14)00078-0
Knihovny.cz E-zdroje
- Klíčová slova
- Click chemistry, Ixodes ricinus, Sialic acid, Thiobarbituric acid assay, Tick, Tick cell line,
- MeSH
- buněčné linie MeSH
- glykoproteiny krev metabolismus MeSH
- interakce hostitele a parazita * MeSH
- klíště metabolismus fyziologie MeSH
- kyselina N-acetylneuraminová metabolismus MeSH
- sliny metabolismus MeSH
- zvířata MeSH
- Check Tag
- ženské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- glykoproteiny MeSH
- kyselina N-acetylneuraminová MeSH
The presence of sialylated structures in tick organs was observed previously using lectin staining. Recently, we demonstrated the presence of sialylated N-glycans using mass spectrometry in tick salivary glands and the gut. However, we proposed a host (blood) origin for these glycans and mapped the transport of sialylated molecules from the gut to the salivary glands. In this report, we performed quantitation of whole sialic acid and of metabolically incorporated sialic acid (N-azido neuraminic acid) in Ixodes ricinus tick samples. We show that the majority of sialylated molecules in the adult tick originate in the host (blood) and are not synthesized by the tick. Similar results were observed for tick cell cultures. The almost complete absence of tick sialylated molecules and the specific transport and localization of host structures into the tick salivary glands and the saliva raises many questions on the role of these molecules in the physiology and, specifically, the blood-feeding of ticks.
Citace poskytuje Crossref.org
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