A searchable database of lectin characterizations, clinical correlates and citations.
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| Source organism|| Elderberry |
| Common nomenclature|| SNA-I,SNA-II, SNA-III, SNA-L, SNA-V, SNA-I', SNA-IV, SNA-Vf, SNA-If |
| Class|| Type 2 RIP derived lectins |
| Index nomenclature|| LECp.Sam.Nig.ba.Csi1 (SNA-I) LECp.Sam.Nig.ba.Csi2 (SNA-I') LECp.Sam.Nig.ba.Cga1 (SNA-V) LECp.Sam.Nig.ba.Hga1 (SNA-II) LECp.Sam.Nig.se.Hga1 (SNA-III) LECp.Sam.Nig.fr.Csi1 (SNA-If) LECp.Sam.Nig.fr.Cga1 (SNA-Vf) LECp.Sam.Nig.fr.Hga1 (SNA-IV) |
| Characterization notes|| For characterization of SNA-II, see: Arch Biochem Biophys. 1990 Mar;277(2):255-62. For characterization of SNA-L, see: Folia Haematol Int Mag Klin Morphol Blutforsch 1980;107(2):299-304 |
| Biological activity|| Blood group A over others. SNA-L shows a preference for blood group H(O) SNA-I agglutinates animal and human erythrocytes. The lectin has a slight preference for type A over type B and type O erythrocytes. See: Biochem J 1984 (221); 163-169 SNA-I inhibits protein synthesis in a rabbit reticulocyte lysate and has RNA N-glycosidase activity. See: J Biol Chem 1987 (262); 1596-1601 SNA-I is slightly toxic for rats and inhibits the growth and development of some insects. See: Digestion 1990 (46);308-316 SNA-I is used for the isolation and fractionation of sialylated oligosaccharides and glycoconjugates. See: Archiv Biochem Biophys 1987 (254);1-8 SNA-I is included in a glycan differentiation kit and is used for the detection of Neu5Ac(x(2,6)Gal/GaINAc sequences in histochemistry and pathology, See: Analytical Biochem 1990 (191);25-30 SNA-V agglutinates rabbit and human erythrocytes. See: Europ J Biochem 1996 (237); 505-5113 The lectin has a slight preference for type B over type A and type O erythrocytes. SNA-V inhibits protein synthesis in animal cell-free systems and has RNA N-glycosidase activity. SNA-V is not toxic to mice. See: Plant Molec Biol 1993 (22); 1181-1186. SNA-II agglutinates animal and human erythrocytes. The lectin has a slight preference for type B over type A and type O erythrocytes. See: Archiv Biochem Biophys 1990 (277);505-513 SNA-II does not inhibit cell-free protein synthesis and has no RNA N-glycosidase activity. Although in nutritional testing with rats the SNA-II preparation used had significant antinutrient effects, this lectin preparation is now known to have been contaminated with Type 2 RIP and therefore it is at present not clear which of the many Sambucus lectins were responsible for the nutritional toxicity. SNA-III agglutinates animal and human erythrocytes. The lectin has a slight preference for type A over type B and type O erythrocytes. See: Carbohydrate Res 1991 (213); 7-17 SNA-HI represents about 0.1% of the seed protein. There are indications that elderberry seeds also contain a Type 2 RIP. See: J. Exper Botany 1994 (45); 513-516 Elderberry fruits contain at least three different lectins. Two of these lectins are Type 2 REP which strongly resemble the bark lectins SNA-I and SNA-V, respectively. The third fruit lectin resembles the bark lectin SNA-II with respect to its molecular structure and specificity but is encoded by a different gene. SNA-If agglutinates animal and human erythrocytes. Its agglutination properties are very similar to those of SNA-I. SNA-If inhibits protein synthesis in a rabbit reticulocyte lysate and has RNA N-glycosidase activity. See: Vam Damme (unpublished results) SNA-Vf agglutinates human and rabbit erythrocytes See: Plant J. 1997 Van Damme, et al. SNA-IV agglutinates rabbit and human erythrocytes. Leaves of elderberry also contain several Type 2 RIP lectins, which have homologues in the bark. |
| Source tissue|| Bark, seeds, leaves |
| Specificity|| SNA-III, SNA-V, SNA-I': GalNAC>Gal |
SNA-Vf, SNA-IV: Gal/GalNAc
SNA-If, SNA-I: NANA (Neu5Ac alpha(2,6)Gal/GalNAc)
| Inhibitors|| Lactose [Gal(beta1-4)Glc] |
| References|| Biochem J 1991 Sep 15;278 ( Pt 3) :667-71