Toxicity and cytotoxicity of nigrin b, a two-chain ribosome-inactivating protein from Sambucus nigra  : comparison with ricin

Battelli, Maria Giulia; Citores, Lucı́a; Buonamici, Laura; Ferreras, José M.; Fm, de Benito; Stirpe, Fiorenzo; Girbés, Tomás

doi:10.1007/s002040050399

Cited by 64 publications

(35 citation statements)

References 21 publications

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“…Our results confirm in the present experimental conditions, the higher toxicity to HeLa cells of volkensin (IC 50 = 3.00 ¥ 10 -13 M [12]) compared to nigrin b and ricin (IC 50 = 5.36 ¥ 10 -8 M and 1.00 ¥ 10 -12 M, respectively [27]). The first step in the study of the interaction of volkensin with cells concerns its binding to glycosylated molecules on the cell membrane through their lectinic B chains.…”

Section: Discussionsupporting

confidence: 88%

“…When cells were incubated at 37°C, volkensin accumulated inside the cell rapidly, the intracellular amount of RIP almost matching the aliquot bound to the cell surface as early as 15 min after incubation. Moreover, cell-bound volkensin did not increase with time while total cell-associated RIP approximately doubled after 1.5 h. The amount of membrane-associated volkensin was 5-and 50-fold less, and that of intracellular volkensin 5-and 60-fold less compared with the corresponding values reported for nigrin b and ricin, respectively [27].…”

Section: Uptake Of Volkensin By Hela Cellsmentioning

confidence: 58%

“…Battelli et al [27] studied the binding to, and the internalization by, HeLa cells of nigrin b and compared it to ricin. Both RIPs initially followed the same pathways, binding to receptors on the cell membrane and reaching an endosomic compartment.…”

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confidence: 99%

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Interaction of volkensin with HeLa cells: binding, uptake, intracellular localization, degradation and exocytosis

Battelli

Musiani

Buonamici

et al. 2004

Cell. Mol. Life Sci.

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Among two-chain ribosome-inactivating proteins (RIPs), volkensin is the most toxic to cells and animals, and is retrogradely axonally transported in the rat central nervous system, being an effective suicide transport agent. Here we studied the binding, endocytosis, intracellular routeing, degradation and exocytosis of this RIP. The interaction of volkensin with HeLa cells was compared to that of nigrin b, as an example of a type 2 RIP with low toxicity, and of ricin, as a reference toxin. Nigrin b and volkensin bound to cells with comparable affinity (approx. 10(-10) M) and had a similar number of binding sites (2 x 10(5)/cell), two-log lower than that reported for ricin. The cellular uptake of volkensin was lower than that reported for nigrin b and ricin. Confocal microscopy showed the rapid localization of volkensin in the Golgi stacks with a perinuclear localization similar to that of ricin, while nigrin b was distributed between cytoplasmic dots and the Golgi compartment. Consistently, brefeldin A, which disrupts the Golgi apparatus, protected cells from the inhibition of protein synthesis by volkensin or ricin, whereas it was ineffective in the case of nigrin b. Of the cell-released RIPs, 57% of volkensin and only 5% of ricin were active, whilst exocytosed nigrin b was totally inactive. Despite the low binding to, and uptake by, cells, the high cytotoxicity of volkensin may depend on (i) routeing to the Golgi apparatus, (ii) the low level of degradation, (iii) rapid recycling and (iv) the high percentage of active toxin remaining after exocytosis.

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Section: Discussionsupporting

confidence: 88%

Section: Uptake Of Volkensin By Hela Cellsmentioning

confidence: 58%

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Interaction of volkensin with HeLa cells: binding, uptake, intracellular localization, degradation and exocytosis

Battelli

Musiani

Buonamici

et al. 2004

Cell. Mol. Life Sci.

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“…A further isoform, α-PAP, is similar in sequence to PAP-S1, and essentially expressed in all organs of the plant [38,39]; it shares 74% identity with PAP. PAP-R has been isolated from the roots of pokeweed plant [40,41] and PAP-H is from hairy roots [40]. Interesting to note that RIP-free callus and suspension cultures of P. americana have been acquired [40,42].…”

Section: Ribosome Inactivating Proteins (Rips)mentioning

confidence: 99%

Potyviral Genome-Linked Protein and its Interaction with Plant Defense Ribosome Inactivating Protein from Phytolacca Americana

Domashevskiy¹

2016

Virol-mycol

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Agriculture is an indispensable part of every person's life, ensuring that nutritious and inexpensive food is readily available. Agriculture continues to be confronted with epidemics, having devastating effects on economies and the plant sources essential for human and animal life. Plants and their pathogens have developed evolutionary adaptations, each shaping the other's defence and invasive strategies. Many different plants produce toxic ribosome inactivating proteins that aid in their defence mechanisms against pathogenic invaders. Viruses must adapt to the host translational machinery, several having evolved to include viral genome-linked proteins that carry numerous viral functions. Here, we review how a potyviral protein from turnip mosaic virus linked to its genome is able to inhibit pokeweed plant defence protein, and perhaps potentially conferring viral resistance to the toxin.

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“…The latter RIPs are referred to as the non-toxic type 2 RIPs. A good example of a RIP that is non-toxic to mammalian cells is SNA-I (Battelli et al, 1997). It is striking that the B-chain of most type 2 RIPs exhibits specificity for galactose and GalNAc, whereas several elderberry RIPs recognize sialic acid .…”

Section: Toxicity Of Elderberry Rip Lectin In Insectsmentioning

confidence: 99%

Entomotoxic action of Sambucus nigra agglutinin i in Acyrthosiphon pisum aphids and Spodoptera exigua caterpillars through caspase‐3‐like‐dependent apoptosis

Shahidi-Noghabi

Damme

Mahdian

et al. 2010

Arch Insect Biochem Physiol

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In this project, the toxicity and mechanism of action of the ricin-B-related lectin SNA-I from elderberry (Sambucus nigra) in the pea aphid (Acyrthosiphon pisum) and the beet armyworm (Spodoptera exigua), two important pest insects in agriculture, were studied. SNA-I is a chimeric lectin belonging to the class of ribosome-inactivating proteins and consists of an A-chain with N-glycosidase activity and a carbohydrate-binding B-chain. Incorporation of 2 mg/ml of SNA-I in the diet of neonates and adults of A. pisum caused 40-46% mortality within 2 days, while in third instars of S. exigua, the larval biomass was significantly reduced by 12% after feeding for 3 days on a diet containing 5 mg/g of SNA-I. Interestingly, extracts of the (mid)gut of treated A. pisum and S. exigua demonstrated DNA fragmentation and this was accompanied with an increase in caspase-3-like activity. The involvement of cell death or apoptosis in the entomotoxicity of SNA-I through induction of caspase-3-like activity was also confirmed by addition of the permeable caspase-3 inhibitor III in the diet, leading to a rescue of the treated aphid neonates. Finally, similar to the chimeric lectin SNA-I, the hololectin SNA-II, consisting of two carbohydrate-binding B-chains caused high mortality to neonate A. pisum aphids with an LC₅₀ of 1.59 mg/ml, suggesting that the entomotoxic action of the lectins under study mainly relies on their carbohydrate-binding activity.

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Toxicity and cytotoxicity of nigrin b, a two-chain ribosome-inactivating protein from Sambucus nigra : comparison with ricin

Cited by 64 publications

References 21 publications

Interaction of volkensin with HeLa cells: binding, uptake, intracellular localization, degradation and exocytosis

Interaction of volkensin with HeLa cells: binding, uptake, intracellular localization, degradation and exocytosis

Potyviral Genome-Linked Protein and its Interaction with Plant Defense Ribosome Inactivating Protein from Phytolacca Americana

Entomotoxic action of Sambucus nigra agglutinin i in Acyrthosiphon pisum aphids and Spodoptera exigua caterpillars through caspase‐3‐like‐dependent apoptosis

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