Elderberries: A Source of Ribosome-Inactivating Proteins with Lectin Activity
Abstract
:1. Introduction: Uses of Sambucus in Ethno-Pharmacology
2. Special Chemical Compounds Found in Sambucus
3. Ribosome-Inactivating Proteins (RIPs)
3.1. Type 1 (Single Chain) Ribosome-Inactivating Proteins
3.1.1. Ebulitins α, β and γ
3.1.2. Nigritins f1 and f2
3.2. Type 2 Ribosome-Inactivating Proteins from S. ebulus L.
3.2.1. Ebulin l
Tissue | Protein | Mr (SDS-PAGE) (kDa) | Sugar Spec. | Yield a | IC50 (nM) | |||
---|---|---|---|---|---|---|---|---|
Whole | A Chain | B Chain | ||||||
A | leaves | ebulin l | 56.0 | 26.0 | 30.0 | Gal | 3.2 | 0.15 |
fruits | ebulin f | 56.0 | 26.0 | 30.0 | Gal | 1.6 | 0.03 | |
blossoms | ebulin blo | 60.0 b | 34.0 | 30.0 | Gal | 5.9 | - | |
rhizome | ebulin r1 | 56.0 | 26.0 | 30.0 | Gal | 1.34 | 0.34 | |
rhizome | ebulin r2 | 56.0 | 26.0 | 30.0 | Gal | 0.56 | 1.14 | |
rhizome | SEA I | 140.0 | 30.0 | 35.0 | Neu5Ac-Gal/GalNAc | 6 | 1 | |
B | bark | nigrin b | 58.0 | 26.0 | 32.0 | Gal/GalNAc | 254 | 0.1 |
bark | basic nigrin b | 64.0 | 32.0 | 32.0 | no determined | 90 | 0.02 | |
bark | SNA-I | 240.0 | 33.0 | 35.0 | Neu5Ac-Gal/GalNAc | 100 | 1.65 | |
bark | SNA-I’ | 120.0 | 32.0 | 35.0 | Neu5Ac-Gal/GalNAc | 0.2 | 1.25 | |
bark | SNRLP1 | 68.0 | 34.0 | 34.0 | GalNAc oligomers | 100 c | 7 | |
bark | SNRLP2 | 62.0 | 30.0 | 32.0 | GalNAc oligomers | - | 7 | |
bark | SNA-V | 120.0 | - | - | Gal/GalNAc | - | - | |
fruits | nigrin f | 58.0 | 26.0 | 31.6 | Gal | 1.3 | 0.03 | |
seeds | nigrin s | 57.3 | 26.0 | 31.0 | Gal | - | - | |
C | bark | sieboldin b | 60.0 | 27.0 | 33.0 | Neu5Ac-Gal/GalNAc | 2.6 | 0.9 |
bark | SSA | 115.4 | 28.7 | 29.0 | Neu5Ac-Gal/GalNAc | - | >100 |
3.2.2. Ebulins r1 and r2
3.2.3. Ebulin f and Polyebulin f
3.2.4. Ebulin Blo
3.2.5. SEA
3.3. Type 2 Ribosome-Inactivating Proteins from Sambucus nigra L.
3.3.1. Nigrin b (SNA-V)
3.3.2. Basic Nigrin b (bNgb)
3.3.3. Nigrin s
3.3.4. Nigrin f
3.3.5. Nigrins l1 and l2
3.3.6. SNA-I
3.3.7. SNA-I’
3.3.8. SNLRP1 and SNLRP2
3.4. Type 2 Ribosome-Inactivating Proteins from S. sieboldiana L.
3.4.1. Sieboldin b
3.4.2. SSA
4. Hololectins of Sambucus
5. Potential Biological Roles of Sambucus Lectins
6. Uses of Ribosome-Inactivating Proteins of Sambucus in Targeted Therapy
7. Toxicity and Histological Analysis of Sambucus Type 2 RIPs Administered at High Concentrations to Mice
7.1. Nigrin b
7.2. Ebulin f
7.3. Ebulin Blo
8. Entomotoxicity of Sambucus Proteins
9. Concluding Remarks
Acknowledgments
Author Contributions
Conflicts of Interest
References
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Tejero, J.; Jiménez, P.; Quinto, E.J.; Cordoba-Diaz, D.; Garrosa, M.; Cordoba-Diaz, M.; Gayoso, M.J.; Girbés, T. Elderberries: A Source of Ribosome-Inactivating Proteins with Lectin Activity. Molecules 2015, 20, 2364-2387. https://doi.org/10.3390/molecules20022364
Tejero J, Jiménez P, Quinto EJ, Cordoba-Diaz D, Garrosa M, Cordoba-Diaz M, Gayoso MJ, Girbés T. Elderberries: A Source of Ribosome-Inactivating Proteins with Lectin Activity. Molecules. 2015; 20(2):2364-2387. https://doi.org/10.3390/molecules20022364
Chicago/Turabian StyleTejero, Jesús, Pilar Jiménez, Emiliano J. Quinto, Damián Cordoba-Diaz, Manuel Garrosa, Manuel Cordoba-Diaz, Manuel J. Gayoso, and Tomás Girbés. 2015. "Elderberries: A Source of Ribosome-Inactivating Proteins with Lectin Activity" Molecules 20, no. 2: 2364-2387. https://doi.org/10.3390/molecules20022364