A novel tunicate (Botryllus schlosseri) putative C-type lectin features an immunoglobulin domain.
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.
Pancer
Z
Z
Institut für Physiologische Chemie, Abteilung für Angewandte Molekularbiologie, Universität, Mainz, Germany.
Diehl-Seifert
B
B
Rinkevich
B
B
Müller
W E
WE
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D018076:DNA, Complementary; D007136:Immunoglobulins / Q000378:metabolism*; D037102:Lectins / Q000235:genetics* / Q000378:metabolism; D037181:Lectins, C-Type; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D014561:Urochordata / Q000235:genetics*
D018076:DNA, Complementary; D007136:Immunoglobulins; D037102:Lectins; D037181:Lectins, C-Type