The tick plasma lectin, Dorin M, is a fibrinogen-related molecule
Language English Country England, Great Britain Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
16551543
DOI
10.1016/j.ibmb.2006.01.008
PII: S0965-1748(06)00009-9
Knihovny.cz E-resources
- MeSH
- Hemocytes chemistry MeSH
- Insect Proteins analysis chemistry physiology MeSH
- Cloning, Molecular MeSH
- Lectins blood chemistry physiology MeSH
- Molecular Sequence Data MeSH
- Ornithodoros metabolism MeSH
- Amino Acid Sequence MeSH
- Base Sequence MeSH
- Sequence Alignment MeSH
- Salivary Glands metabolism MeSH
- Protein Structure, Tertiary MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Insect Proteins MeSH
- Lectins MeSH
A lectin, named Dorin M, previously isolated and characterized from the hemolymph plasma of the soft tick, Ornithodoros moubata, was cloned and sequenced. The immunofluorescence using confocal microscopy revealed that Dorin M is produced in the tick hemocytes. A tryptic cleavage of Dorin M was performed and the resulting peptide fragments were sequenced by Edman degradation and/or mass spectrometry. Two of three internal peptide sequences displayed a significant similarity to the family of fibrinogen-related molecules. Degenerate primers were designed and used for PCR with hemocyte cDNA as a template. The sequence of the whole Dorin M cDNA was completed by the method of RACE. The tissue-specific expression investigated by RT-PCR revealed that Dorin M, in addition to hemocytes, is significantly expressed in salivary glands. The derived amino-acid sequence clearly shows that Dorin M has a fibrinogen-like domain, and exhibited the most significant similarity with tachylectins 5A and 5B from a horseshoe crab, Tachypleus tridentatus. In addition, other protein and binding characteristics suggest that Dorin M is closely related to tachylectins-5. Since these lectins have been reported to function as non-self recognizing molecules, we believe that Dorin M may play a similar role in an innate immunity of the tick and, possibly, also in pathogen transmission by this vector.
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
GENBANK
AY333989
