European Journal of Biochemistry vol:237 issue:2 pages:505-13
The molecular structure of the Sambucus nigra agglutinin V (SNAV), which has been described previously as a type-2 ribosome-inactivating protein called nigrin b, has been studied in detail by analysis of the purified protein combined with cDNA cloning and molecular modelling. Native SNAV is a dimer of two [A-s-s-B] pairs. Hapten inhibition assays indicated that GalNAc is a 20-fold more potent inhibitor of SNAV than Gal. A cDNA clone encoding SNAV was isolated from a cDNA library constructed with mRNA from the bark. Sequence analysis of this cDNA revealed a striking similarity to the recently cloned NeuAc alpha-2,6-gal/GalNAc-specific S. nigra bark agglutinin I (SNAI) and to the previously sequenced type-2 ribosome-inactivating proteins from Ricinus communis and Abrus precatorius. In addition, molecular modelling of SNAV further suggested that its structure closely resembles that of ricin. The N-terminal sequence of the B chain of SNAV also shows a marked similarity with the polypeptide of the previously described GalNAc-specific s. nigra bark agglutinin II (SNAII), which unlike SNAV and SNAI has no ribosome-inactivating activity. It appears, therefore, that elderberry bark contains at least two different type-2 ribosome-inactivating proteins and a lectin built up of subunits which are closely related to the B chain of SNAV.