Presence of polymerized and free forms of the non-toxic type 2 ribosome-inactivating protein ebulin and a structurally related new homodimeric lectin in fruits of Sambucus ebulus L.

Planta ◽  
1998 ◽  
Vol 204 (3) ◽  
pp. 310-317 ◽  
Author(s):  
Lucía Citores ◽  
Fernando M. de Benito ◽  
Rosario Iglesias ◽  
J. Miguel Ferreras ◽  
Pablo Argüeso ◽  
...  
Keyword(s):  
Ribosome Inactivating Protein ◽  
Sambucus Ebulus

scholarly journals Ebulin 1, a nontoxic novel type 2 ribosome-inactivating protein from Sambucus ebulus L. leaves.

1993 ◽  
Vol 268 (24) ◽  
pp. 18195-18199
Author(s):  
T. Girbés ◽  
L. Citores ◽  
R. Iglesias ◽  
J.M. Ferreras ◽  
R. Muñoz ◽  
...  
Keyword(s):  
Ribosome Inactivating Protein ◽  
Sambucus Ebulus

Fruticulosin: A novel type 2 ribosome-inactivating protein from Abrus fruticulosus seeds that exhibits toxic and antileishmanial activity

2018 ◽  
Vol 658 ◽  
pp. 46-53
Author(s):  
Mayron Alves de Vasconcelos ◽  
Samara Sena da Penha ◽  
Vinícius Rodrigues Castro e Silva ◽  
Talita Abrante Leite ◽  
Elnatan Bezerra de Souza ◽  
...  
Keyword(s):  
Antileishmanial Activity ◽  
Ribosome Inactivating Protein

scholarly journals Mutational analysis of the carbohydrate-binding activity of the NeuAc(α-2,6)Gal/GalNAc-specific type 2 ribosome-inactivating protein from elderberry (Sambucus nigra) fruits

2002 ◽  
Vol 364 (2) ◽  
pp. 587-592 ◽  
Author(s):  
Ying CHEN ◽  
Pierre ROUGE ◽  
Willy J. PEUMANS ◽  
Els J.M. van DAMME
Keyword(s):  
Mutational Analysis ◽  
Binding Activity ◽  
Site Directed Mutagenesis ◽  
Carbohydrate Binding ◽  
Ribosome Inactivating Protein ◽  
Sambucus Nigra ◽  
Original Activity ◽  
Highly Active ◽  
Critical Residue

Sambucus nigra agglutinin I (SNA-I) is a type 2 ribosome-inactivating protein. Site-directed mutagenesis was used to mimic the conversion of the highly active B-chain of fruit-specific SNA (SNA-If) into the completely inactive B-chain of the closely related and naturally occurring loss-of-activity mutant called S. nigra agglutinin lectin-related protein. In the first mutant SNA-If-M1 the high-affinity site 2 of SNA-If was disrupted by replacing the presumed critical residue Asp231 with Glu231. In the double mutant SNA-If-M2, site 1 of SNA-If-M1 was also disrupted by substituting the presumed critical residue Asn48 with Ser48. The parent type 2 ribosome-inactivating protein and both mutants were expressed in Nicotiana tabacum Samsun NN and the recombinant proteins were purified and analysed. Recombinant SNA-If agglutinated rabbit erythrocytes equally well as SNA-If, but both mutants were completely inactive in this test. Binding assays to immobilized galactose and fetuin revealed that the mutation Asp231→Glu231 reduces the affinity of the B-chain for galactose and fetuin by more than 50%. Furthermore, the introduction of the second mutation Asn48→Ser48 reduces the binding activity to less than 20% of the original activity.

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