A non-toxic two-chain ribosome-inactivating protein co-exists with a structure-related monomeric lectin (SNA III) in elder (<i>Sambucus nigra</i>) fruits

Girbés, Tomás; Citores, Lucı́a; Benito, F M de; Inglesias, R; Ferreras, José M.

doi:10.1042/bj3150343

Cited by 24 publications

(34 citation statements)

References 14 publications

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“…Other procedures: In-vitro translation, 28 S rRNA N-glycosidase activity, N-terminal amino acid sequence, SDS-PAGE and glycan chain detection were carried out as described elsewhere (GirbeÂ s et al 1993b;Rojo et al 1994). Red-blood-cell agglutination was carried out at room temperature on microtiter plates containing 100 ll of 5 mM sodium phosphate (pH 7.5), 0.14 M NaCl and 0.5% of red blood cells.…”

Section: Methodsmentioning

confidence: 99%

“…By contrast, type 2 RIPs such as ricin, abrin, modeccin, volkensin and viscumin may be highly toxic or non toxic, such as nigrin b (GirbeÂ s et al 1993a) and ebulin 1 (GirbeÂ s et al 1993b).…”

Section: Introductionmentioning

confidence: 99%

“…Recently, we have reported that Sambucus species contain both type 1 RIPs ebulitins (de Benito et al 1995) and the type 2 RIPs ebulin 1 (GirbeÂ s et al 1993b) and nigrin b (GirbeÂ s et al 1993a), that display the novelty of being non-toxic to both human cultured cells and to mice. In addition, Sambucus nigra agglutinin (SNA) I has been reported as a true eight-chain type 2 RIP (Van Damme et al 1996a) and the genes of SNA I and nigrin b have been cloned (Van Damme et al 1996a, b).…”

Section: Introductionmentioning

confidence: 99%

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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.

Citores

Iglesias

et al. 1998

Planta

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Mature leaves of dwarf elder (Sambucus ebulus L.) contain the non-toxic type 2 ribosome-inactivating protein ebulin 1 (Girbés et al., 1993b, J. Biol. Chem. 268: 18195-18199). We have now found that the green fruits of dwarf elder contain both free and polymerized forms of ebulin (ebulin f) and a new homodimeric D-galactose-binding lectin (SELfd). Polymerized material containing ebulin and lectin is composed of aggregates of variable relative molecular mass, some of them being close to 250,000. These aggregate forms are maintained in part by reducible disulphide bridges and reconstitute from reductant-free dialyzed material previously reduced with 2-mercaptoethanol. Direct incubation of free ebulin f with the free SELfd did not lead to polymerization, thus indicating that polymerization triggers some kind of substantial and perhaps catalyzed change in the structure of these proteins. Ebulin-containing polymerized material reacts with anti-ebulin f antibodies. Our results indicate that ebulin f is a fruit-form of ebulin 1. In contrast to green fruits, mature fruits lack both polymerized material and ebulin f, thus indicating some kind of reserve role for them in green fruits. Polymerization of ebulin and the dimeric lectin may represent a novel means of storing the non-toxic type 2 ribosome-inactivating proteins and lectins found in highly metabolic tissues, such as green fruits.

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Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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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.

Citores

Iglesias

et al. 1998

Planta

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“…Typical GalNAc-specific type 2 RIP were first isolated from the bark of elderberry (Sumbucus nigru) (Girbes et al, 1993a;Van Damme et a]., 1996a) and leaves of dwarf elder (S. ebulus) (Girbes et al, 1993b). More recently, similar type 2 RIP were also found in the seeds and fruits of S. nigru (Citores et al, 1994Girbes et al, 1996). In addition, molecular cloning of the previously described NeuSAc(a2,6)Gal/GalNAcspecific agglutinins from S. rzigru and S. sieboldiuna (SNAI and SSAI, respectively) revealed that these lectins also are type 2 RIP.…”

mentioning

confidence: 87%

Elderberry (Sambucus Nigra) Bark Contains two Structurally Different Neusac(α2,6)Gal/Galnac‐Binding Type 2 Ribosome‐Inactivating Proteins

Damme

Roy

Barre

et al. 1997

European Journal of Biochemistry

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A second NeuAc(a2,6)Gal/GalNAc binding type 2 ribosome-inactivating protein (RIP), called SNAI' has been isolated from elderberry (Sumbucus nigru) bark. SNAI' is a minor bark protein which closely resembles the previously described major Neu5Ac(a2,6)Gal/GalNAc binding type 2 RIP called SNAI with respect to its carbohydrate-binding specificity and ribosome-inactivating activity but has a different molecular structure. Molecular cloning revealed that the deduced amino acid sequence of SNAI' is highly similar to that of SNAI and that the difference in molecular structure between both proteins relies on a single cysteine residue present in the B chain of SNAI but absent from SNAI'. The isolation of SNAI' not only identifies a minor bark protein as a type 2 RIP but also further emphasizes the complexity of the type 2 RIP/lectin mixture present in the bark of elderberry.

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“…Among plants, the genus Sambucus seems to be paradigmatic since it contains a complex mixture of lectins and ribosome-inactivating proteins with yet an unexplained biological role (Ferreras et al, 2000;Girbes et al, 2004). S. nigra, S. ebulus, S. racemosa and S. sieboldiana contain monomeric, dimeric and tetrameric lectins and also a kind of type 2 RIPs with the special feature of being non-toxic to whole cells and animals, namely nigrins (Girbes et al, 1993b(Girbes et al, , 1996Citores et al, 1994), ebulins (Girbes et al, 1993c;Citores et al, 1997) and sieboldin (Rojo et al, 1997). Their lack of toxicity has been attributed to defective B-chains with reduced affinity for galactosides (Pascal et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

Transient occurrence of an ebulin-related d-galactose-lectin in shoots of Sambucus ebulus L.

Citores

Jiménez

et al. 2008

Phytochemistry

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A non-toxic two-chain ribosome-inactivating protein co-exists with a structure-related monomeric lectin (SNA III) in elder (Sambucus nigra) fruits

Cited by 24 publications

References 14 publications

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.

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.

Elderberry (Sambucus Nigra) Bark Contains two Structurally Different Neusac(α2,6)Gal/Galnac‐Binding Type 2 Ribosome‐Inactivating Proteins

Transient occurrence of an ebulin-related d-galactose-lectin in shoots of Sambucus ebulus L.

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