6533b7defe1ef96bd1276736
RESEARCH PRODUCT
A novel tunicate (Botryllus schlosseri) putative C-type lectin features an immunoglobulin domain.
Werner E. G. MüllerZeev PancerBaruch RinkevichBärbel Diehl-seifertsubject
DNA ComplementaryMolecular Sequence DataImmunoglobulinsBotryllus schlosseriImmunoglobulin domainC-type lectinLectinsGeneticsAnimalsLectins C-TypeAmino Acid SequenceUrochordataMolecular Biologychemistry.chemical_classificationbiologyBase SequenceSequence Homology Amino AcidCD69LectinCell BiologyGeneral Medicinebiology.organism_classificationMolecular biologyAmino acidTunicateKLRB1chemistrybiology.proteindescription
We have cloned a putative C-type lectin of Botryllus schlosseri [Ascidiacea], whose deduced protein of 333 amino acids features three building blocks: (i) a Greek-key motif signature at the amino-terminus, (ii) a C-type lectin domain signature, and (iii) an immunoglobulin (Ig) domain at the carboxyl terminus. This C-type lectin was termed BSCLT. Similarity searches revealed that the Ig domain in BSCLT, which is evidently not polymorphic, is best classified as an Intermediate-type Ig domain. Rabbit antibodies, raised against recombinant BSCLT, cross-reacted in a Western blot with a 38-kD polypeptide in tunicate crude extract. Presumably, this bimodal tunicate protein is the first description of a soluble lectin that features besides the carbohydrate recognition domain also a complete Ig domain.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1997-06-01 | DNA and cell biology |