Molecular Cloning of Two Different Mannose-Binding Lectins from Tulip Bulbs

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/65309/1/j.1432-1033.1996.00419.x.pd

The NeuAc(alpha-2,6)Gal/GalNAc-binding lectin from elderberry (Sambucus nigra) bark, a type-2 ribosome-inactivating protein with an unusual specificity and structure

The cDNA encoding the NeuAc(alpha-2,6)Gal/GalAc 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(alpha-2,6)Gal/GalNAc and its unusual molecular structure