Isolation and characterization of a new non-toxic two-chain ribosome-inactivating protein from fruits of elder (<i>Sambucus nigra</i>L.)

Citores, Lucı́a; Benito, F M de; Iglesias, Rosario; Ferreras, José M.; Jiménez, Pilar; Argüeso, Pablo; Farías, Gustavo; Méndez, Enrique; Girbés, Tomás

doi:10.1093/jxb/47.10.1577

Cited by 31 publications

(24 citation statements)

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“…The methodological core of the affinity method for the preparation of nigrin was its binding to a D-galactose matrix obtained by acid treatment of Sepharose 6B. Further elution with either lactose or D-galactose allowed the isolation of D-galactose-binding proteins (Barbieri, Zamboni, Montanaro, Sperti, & Stirpe, 1980;Citores et al, 1996;Olsnes, Stirpe, Sandvig, & Pihl, 1982). Nonetheless, it was observed that nigrin binding to the acid-modified beads to a variable extent depended on the temperature.…”

Section: Discussionmentioning

confidence: 99%

Occurrence and new procedure of preparation of nigrin, an antiribosomal lectin present in elderberry bark

Ferreras

Citores

Iglesias

et al. 2011

Food Research International

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Section: Discussionmentioning

confidence: 99%

Occurrence and new procedure of preparation of nigrin, an antiribosomal lectin present in elderberry bark

Ferreras

Citores

Iglesias

et al. 2011

Food Research International

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“…(1991) and consisted of two isoforms. This was subsequently found to be a type 2 RIP and named nigrin‐f (Citores et al . 1996; Girbés et al .…”

Section: Structure and Physiologymentioning

confidence: 99%

Sambucus nigraL.

Atkinson

2002

Journal of Ecology

138

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“…The structure of these lectins also showed a large homology with that of the B chain of type 2 RIPs [49]. Monomeric lectins are present in the leaves [45] and rhizomes [29] of S. ebulus , in the leaves [37], bark [46], fruits [47] and seeds [48] of S. nigra , and in the bark of S. sieboldiana [49] and S. racemosa [39]. The homodimeric lectins are found in leaves [50] and fruits [30] from S. ebulus and leaves [37] from S. nigra .…”

Section: Ribosome Inactivating Proteins From Sambucusmentioning

confidence: 99%

Use of Ribosome-Inactivating Proteins from Sambucus for the Construction of Immunotoxins and Conjugates for Cancer Therapy

Ferreras

Citores

Iglesias

et al. 2011

Toxins

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The type 2 ribosome-inactivating proteins (RIPs) isolated from some species belonging to the Sambucus genus, have the characteristic that although being even more active than ricin inhibiting protein synthesis in cell-free extracts, they lack the high toxicity of ricin and related type 2 RIPs to intact cells and animals. This is due to the fact that after internalization, they follow a different intracellular pathway that does not allow them to reach the cytosolic ribosomes. The lack of toxicity of type 2 RIPs from Sambucus make them good candidates as toxic moieties in the construction of immunotoxins and conjugates directed against specific targets. Up to now they have been conjugated with either transferrin or anti-CD105 to target either transferrin receptor- or endoglin-overexpressing cells, respectively.

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Isolation and characterization of a new non-toxic two-chain ribosome-inactivating protein from fruits of elder (Sambucus nigraL.)

Cited by 31 publications

References 54 publications

Occurrence and new procedure of preparation of nigrin, an antiribosomal lectin present in elderberry bark

Occurrence and new procedure of preparation of nigrin, an antiribosomal lectin present in elderberry bark

Sambucus nigraL.

Use of Ribosome-Inactivating Proteins from Sambucus for the Construction of Immunotoxins and Conjugates for Cancer Therapy

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