Isolation and characterization of Dorin M, a lectin from plasma of the soft tick Ornithodoros moubata
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
10732987
DOI
10.1016/s0965-1748(99)00107-1
PII: S0965174899001071
Knihovny.cz E-resources
- MeSH
- Hemagglutination Tests MeSH
- Ticks chemistry MeSH
- Lectins chemistry immunology isolation & purification MeSH
- Mice MeSH
- Hemagglutination Inhibition Tests MeSH
- Animals MeSH
- Check Tag
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Lectins MeSH
A lectin with high hemagglutinating activity, which we have named Dorin M, was identified in the plasma of the soft tick Ornithodoros moubata. The activity of the plasma lectin could be efficiently inhibited by sialic acid, N-acetyl-D-hexosamines and sialoglycoproteins. Dorin M was purified to homogeneity using two different isolation systems: affinity chromatography on a column of bovine submaxillary mucin conjugated to Sepharose 4B with specific elution by N-acetyl-D-glucosamine and chromatography on Blue-Sepharose followed by anion exchange FPLC on a MonoQ column. The purified lectin is a glycoprotein which, in the native state, forms aggregates with molecular mass of about 640 kDa. Non-reducing SDS PAGE revealed that the lectin consists of two noncovalently bound subunits migrating closely around 37 kDa. Dorin M is a glycoprotein, probably modified by N-type glycosylation. After chemical deglycosylation, only one band of about 32 kDa was detected. Dorin M is the first lectin purified from ticks.
References provided by Crossref.org
Tick Immune System: What Is Known, the Interconnections, the Gaps, and the Challenges
A bite so sweet: the glycobiology interface of tick-host-pathogen interactions
Interaction of the tick immune system with transmitted pathogens
Fibrinogen-related proteins in ixodid ticks
