Open AccessThe NeuAc(α‐2,6)‐Gal/GalNAc‐Binding Lectin from Elderberry ( Sambucus Nigra ) Bark, a type‐2 Ribosome‐Inactivating Protein with an Unusual Specificity and Structure
Author(s) -
Damme Els J. M.,
Barre Annick,
Rougé Pierre,
Leuven Fred,
Peumans Willy J.
Publication year - 1996
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1996.00128.x
Subject(s) - sambucus nigra , ribosome inactivating protein , ricin , lectin , complementary dna , biology , reticulocyte , microbiology and biotechnology , c type lectin , cdna library , abrus precatorius , ribosome , biochemistry , agglutinin , cd69 , messenger rna , gene , genetics , rna , toxin , cytotoxic t cell , il 2 receptor , in vitro
The cDNA encoding the NeuAc(α‐2,6)Gal/GalNAc binding lectin from elderberry ( Sambucus nigra ) bark (SNAI) was isolated from a cDNA library constructed with mRNA from the bark. Sequence analysis of this lectin cDNA revealed a striking similarity to the previously sequenced type‐2 ribosome‐inactivating proteins from Ricinus communis and Abrus precatorius. Molecular modelling of SNAI further indicated that its structure closely resembles that of ricin. Since SNAI strongly inhibits cell‐free protein synthesis in a rabbit reticulocyte lysate it presumably is a type‐2 ribosome‐inactivating protein. However, SNAI differs from all previously described type‐2 ribosome‐inactivating proteins by its specificity towards NeuAc(α‐2,6)Gal/GalNAc and its unusual molecular structure.