Characterization of highly toxic type 2 ribosome-inactivating proteins from Adenia lanceolata and Adenia stenodactyla (Passifloraceae)

Stirpe, Fiorenzo; Bolognesi, Andrea; Bortolotti, Massimo; Farini, Valentina; Lubelli, Chiara; Pelosi, Emanuele; Polito, Letizia; Dozza, Barbara; Strocchi, Paola; Chambery, Angela; Parente, Augusto; Barbieri, Luigi

doi:10.1016/j.toxicon.2007.02.020

Cited by 43 publications

(42 citation statements)

References 43 publications

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“…Gout and cow erythrocytes were not agglutinated by any lectin; treatment of RBCs with trypsin did not bring about any difference (Table ). Most of type‐II RIPs are Gal/GalNAc‐specific including Cucurbitaceae family members, with exception for Sambucus nigra agglutinin‐1 that preferentially binds sialylated glycans and Iris bulb (IRAb) that is specific for Gal/GalNAc and unexpectedly interacts to mannose . MBaLs isolectins are no exceptions to their family members, as they get inhibited by d ‐galactose and GalNAc.…”

Section: Resultsmentioning

confidence: 99%

Isolation and partial characterization of 3 nontoxic d‐galactose–specific isolectins from seeds of Momordica balsamina

Awadallah

Osman

Ibrahim

et al. 2016

J of Molecular Recognition

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Three isolectins denoted hereforth MBaL-30, MBaL-60, and MBaL-80 were isolated from seeds extract of Momordica balsamina by 30%, 60%, and 80% ammonium sulfate saturations, respectively. The native molecular weights of these lectins, as judged by gel filtration, were 108, 56, and 160 kDa, respectively. On SDS-PAGE, under reduced condition, 27 kDa band was obtained for all isolectins. The lectins hemagglutinating activities were variably inhibited by d-galactose (minimum inhibitory concentrations = 12.5mM, 50mM, and 0.391mM, respectively). MBaL-30 and -60 could agglutinate all human blood types with slight preference for the A and O blood groups, whereas MBaL-80 did not agglutinate B and AB blood types. The 3 isolectins were purified from crude seeds extract, collectively, in a single step on the affinity matrix Lactamyl-Seralose 4B; this purified lectin fraction, which contains all isolectins, is termed MBaL. The N-terminal of MBaL till the 25th amino acid was NLSLSELDFSADTYKSFIKNLRKQL, which shares 88% sequence identity with Momordica charantia lectin type-2 ribosomal inactivating protein from Momordica charantia and 50% with momordin II from Momordica balsamina. MBaL retained 100% activity at up to 50°C for 30 minutes. MBaL-30 and MBaL-60 exhibited maximum activities in the pH range between 4 and 8, while MBaL-80 was showing maximum activity in the pH range between 3 and 5. Treatment of MBaL-30 and MBaL-60 with EDTA completely abolished their hemagglutinating activities. Addition of Zn and Fe ions to the ethylenediaminetetraacetic acid-treated MBaL-30 and MBaL-60 lectins did not only regained the loss of activity but also resulted in 200% to 300% increase in activity, respectively. MBaL-30 and -60 agglutinated gram positive Listeria monocytogenes and Staphylococcus aureus, whereas MBaL-30 could merely agglutinate Escherichia coli. None of these lectins could arrest bacterial growth. Addition of MBaL to cancer cell lines (Gastric cancer cell line (AGS) and Gastric cencer cell line (MKN45), Glioblastoma (ECV-304), and Human urinary bladder cancer cell line (U87-MG)) at varying concentrations did not cause statistically significant changes on cell growth and viability.

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Section: Resultsmentioning

confidence: 99%

Isolation and partial characterization of 3 nontoxic d‐galactose–specific isolectins from seeds of Momordica balsamina

Awadallah

Osman

Ibrahim

et al. 2016

J of Molecular Recognition

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“…Therefore, partial, mild hydrolysis of Sepharose by acid treatment -for example incubation in 1 M HCl for three hours at 50 °C (Voss et al, 2006) -can be used to cleave the polysaccharide chains, thus exposing additional terminal galactosyl residues, without completely degrading the Sepharose (Ersson et al, 1973;Lis & Sharon, 1981). Recently, numerous lectins have been isolated on acid treated Sepharose (Jimbo et al, 2000;Kawagishi et al, 1994;Mishra et al, 2004;Stirpe et al, 2007;Voss et al, 2006).…”

Section: Adsorbent Matricesmentioning

confidence: 99%

Affinity Chromatography of Lectins

Pohleven¹,

Štrukelj²,

Kos³

2012

Affinity Chromatography

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“…The mechanism (ribosome-inactivating effects) of the toxicity of pulchellin is similar to that of ricin and abrin introduced above with some variations (also see Araújo et al, 2010;Castilho et al, 2008;Silva et al, 2005). Stirpe et al (2007) isolated, purified and identified stenodactylin and lanceolin [which are highly toxic to cells (in which they induce apoptosis) and to mice] from the caudices of Passifloraceae Adenia lanceolata and A. stenodactyla, respectively. The same authors also found that stenodactylin and lanceolin agglutinate red blood cells, inhibit protein synthesis both by a cell-free system and by whole cells, and depurinate ribosomes and DNA, but not tRNA or poly (A).…”

Section: Pulchellinmentioning

confidence: 99%

Toxicological studies on plant proteins: a review

Sun

2011

J of Applied Toxicology

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Nowadays, toxicological studies are contributing to human health more than ever. Reports on the toxicological studies of plant proteins, which are continuously growing in number in the literature, have been reviewed. Two important aspects are discussed: dietary safety evaluation, including toxicity tests and the maximum daily intake allowance, and the appropriate proportion in our daily diets of proteins from traditional foods and of new proteins from plant sources not traditionally employed as foods. Water hyacinth leaf proteins, sweet lupin proteins and canola proteins have not been shown to be toxic, although they are not traditionally employed as food proteins. These findings are very important for exploiting valuable new protein sources that are suitable for human or animal consumption and applicable to the food industry. Acutely toxic proteins, including lectins, ribosome-inactivating proteins, inhibitors of proteolytic enzymes and glycohydro-lases, have been isolated from plant materials and identified. Their toxicities and molecular characteristics have been described. The toxicity of proteins depends upon their specific native structures. Once they are denatured by appropriate treatment, such as heating, their toxicity can be reduced or even eliminated. These findings indicate that raw materials that contain this kind of toxic protein are not edible. However, after proper processing, they may be suitable for human or animal consumption. Although the toxicities of type 2 ribosome-inactivating proteins reported by different authors vary, the maximum dosages are still trace amounts.

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Characterization of highly toxic type 2 ribosome-inactivating proteins from Adenia lanceolata and Adenia stenodactyla (Passifloraceae)

Cited by 43 publications

References 43 publications

Isolation and partial characterization of 3 nontoxic d‐galactose–specific isolectins from seeds of Momordica balsamina

Isolation and partial characterization of 3 nontoxic d‐galactose–specific isolectins from seeds of Momordica balsamina

Affinity Chromatography of Lectins

Toxicological studies on plant proteins: a review

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