A Novel Tunicate (Botryllus schlosseri) Putative C-Type Lectin Features an Immunoglobulin Domain

ZEEV PANCER, BÄRBEL DIEHL-SEIFERT, BARUCH RINKEVICH, WERNER E.G. MÜLLER

Research output: Contribution to journalArticlepeer-review

Abstract

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.
Original languageEnglish
Pages (from-to)801-806
Number of pages6
JournalDNA and Cell Biology
Volume16
Issue number6
DOIs
StatePublished - 1997
Externally publishedYes

Bibliographical note

doi: 10.1089/dna.1997.16.801

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