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

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

doi:10.1089/dna.1997.16.801

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 journal › Article › peer-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 language	English
Pages (from-to)	801-806
Number of pages	6
Journal	DNA and Cell Biology
Volume	16
Issue number	6
DOIs	https://doi.org/10.1089/dna.1997.16.801
State	Published - 1997
Externally published	Yes

Bibliographical note

doi: 10.1089/dna.1997.16.801

ASJC Scopus subject areas

Molecular Biology
Genetics
Cell Biology

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10.1089/dna.1997.16.801

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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.",

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AU - DIEHL-SEIFERT, BÄRBEL

AU - RINKEVICH, BARUCH

AU - MÜLLER, WERNER E.G.

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AB - 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.

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

Abstract

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