Recombinant pebulin protein, a type 2 ribosome-inactivating protein isolated from dwarf elder (Sambucus ebulus L.) shows anticancer and antifungal activities in vitro

Rezaei-Moshaei, Masoumeh; Dehestani, Ali; Bandehagh, Ali; Parizi, Ali Pakdin; Golkar, Majid; Heidari-Japelaghi, Reza

doi:10.1016/j.ijbiomac.2021.01.129

Cited by 11 publications

(3 citation statements)

References 55 publications

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“…In this case, no inhibition halo was observed in either strain (Table 4) even though a slight effect on fungal growth was observed for both the C. parasitica strain E4 and strain E13 (Figure S7). In this framework, these data confirm that quinoin possesses antifungal activity although to a lesser extent, as reported for other RIPs against hyphomycete fungi such as Verticillium dahlia, Alternaria solani, Fusarium oxysporum solani [43][44][45] and other fungal genera [11].…”

Section: Antimicrobial Activitysupporting

confidence: 84%

The Structural Characterization and Antipathogenic Activities of Quinoin, a Type 1 Ribosome-Inactivating Protein from Quinoa Seeds

Ragucci

Bulgari

Russo

et al. 2021

IJMS

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Quinoin is a type 1 ribosome-inactivating protein (RIP) we previously isolated from the seeds of pseudocereal quinoa (Chenopodium quinoa) and is known as a functional food for its beneficial effects on human health. As the presence of RIPs in edible plants could be potentially risky, here we further characterised biochemically the protein (complete amino acid sequence, homologies/differences with other RIPs and three-dimensional homology modeling) and explored its possible defensive role against pathogens. Quinoin consists of 254 amino acid residues, without cysteinyl residues. As demonstrated by similarities and homology modeling, quinoin preserves the amino acid residues of the active site (Tyr75, Tyr122, Glu177, Arg180, Phe181 and Trp206; quinoin numbering) and the RIP-fold characteristic of RIPs. The polypeptide chain of quinoin contains two N-glycosylation sites at Asn115 and Asp231, the second of which appears to be linked to sugars. Moreover, by comparative MALDI-TOF tryptic peptide mapping, two differently glycosylated forms of quinoin, named pre-quinoin-1 and pre-quinoin-2 (~0.11 mg/100 g and ~0.85 mg/100 g of seeds, respectively) were characterised. Finally, quinoin possesses: (i) strong antiviral activity, both in vitro and in vivo towards Tobacco Necrosis Virus (TNV); (ii) a growth inhibition effect on the bacterial pathogens of plants; and (iii) a slight antifungal effect against two Cryphonectria parasitica strains.

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Section: Antimicrobial Activitysupporting

confidence: 84%

The Structural Characterization and Antipathogenic Activities of Quinoin, a Type 1 Ribosome-Inactivating Protein from Quinoa Seeds

Ragucci

Bulgari

Russo

et al. 2021

IJMS

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“…Among the several options of bacteria host, E. coli BL21(DE3)pLysS was chosen for this study due to its chromosomal copy of the gene for T7 RNA polymerase (Rezaei-Moshaei et al 2021). The host cells were lysogens of bacteriophage DE3 that carried the gene for T7 RNA polymerase under lacUV5 control.…”

Section: Discussionmentioning

confidence: 99%

The recombinant expression and antimicrobial activity determination of Cecropin-like part of Heteroscorpine-1 from Heterometrus laoticus

Erviana

SAENGKUN²,

RUNGSA³

et al. 2022

Biodiversitas

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Abstract. Erviana R, Saengkun Y, Rungsa P, Jangpromma N, Mustofa, Daduang S. 2022. The recombinant expression and antimicrobial activity determination of Cecropin-like part of Heteroscorpine-1 from Heterometrus laoticus. Biodiversitas 23: 5646-5653. Antimicrobial peptides are promising novel antibiotics that hold great potential in combating bacteria, fungi, viruses, and parasites. Recent interest has increased in their potential as new pharmacological agents. Large quantities of antimicrobial peptides are required in order to fulfill the demand for the peptides for scientific research and clinical trials. Gene expression systems for antimicrobial peptides have been developed, which may be utilized efficiently for various antimicrobial peptide-related studies and applications. However, many expression systems that have been developed require many steps that impact the expression cost. This study established the fast and easy expression system of recombinant Cecropin-like part of Heteroscorpine-1 (CeHS-1) and determined their activity. The gene was chemically synthesized, ligated to the expression vector pET32a, transformed to Escherichia coli BL21 (DE3) pLysS competent cell, and induced by 0.2 mM isopropyl ?-D-1-thiogalactopyranoside. The induction time optimization determined that the 3 hrs induction resulted in the highest peptides yield. The prolonged induction would decrease the peptides yield due to the toxicity of the peptides toward the host cells. The peptide purification was facilitated by His tag sequence through purifying the affinity chromatographic column of Ni-NTA. The induction was able to express the expected peptides in the soluble fraction. The antimicrobial activity assay showed that the recombinant peptides could inhibit the growth of many bacterial strains. However, their activity was lower compared to the synthetic peptides. This finding demonstrated that the developed expression system in this study might facilitate the easy and feasible expression system for CeHS-1. Additionally, the study revealed that the antimicrobial activity of the expressed peptides could be preserved.

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“…The only type 2 RIP reported to have antifungal activity is pebulin, a recombinant protein from Sambucus ebulus L. This protein was able to completely inhibit the germination of A. solani and Fusarium oxysporum Schltdl. spores at a concentration of 5 µg/mL [ 102 ].…”

Section: Inhibition Of Fungal Growth By Ripsmentioning

confidence: 99%

Antifungal Activity of Ribosome-Inactivating Proteins

Iglesias,

Citores,

Gay

et al. 2024

Toxins

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The control of crop diseases caused by fungi remains a major problem and there is a need to find effective fungicides that are environmentally friendly. Plants are an excellent source for this purpose because they have developed defense mechanisms to cope with fungal infections. Among the plant proteins that play a role in defense are ribosome-inactivating proteins (RIPs), enzymes obtained mainly from angiosperms that, in addition to inactivating ribosomes, have been studied as antiviral, fungicidal, and insecticidal proteins. In this review, we summarize and discuss the potential use of RIPs (and other proteins with similar activity) as antifungal agents, with special emphasis on RIP/fungus specificity, possible mechanisms of antifungal action, and the use of RIP genes to obtain fungus-resistant transgenic plants. It also highlights the fact that these proteins also have antiviral and insecticidal activity, which makes them very versatile tools for crop protection.

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Recombinant pebulin protein, a type 2 ribosome-inactivating protein isolated from dwarf elder (Sambucus ebulus L.) shows anticancer and antifungal activities in vitro

Cited by 11 publications

References 55 publications

The Structural Characterization and Antipathogenic Activities of Quinoin, a Type 1 Ribosome-Inactivating Protein from Quinoa Seeds

The Structural Characterization and Antipathogenic Activities of Quinoin, a Type 1 Ribosome-Inactivating Protein from Quinoa Seeds

The recombinant expression and antimicrobial activity determination of Cecropin-like part of Heteroscorpine-1 from Heterometrus laoticus

Antifungal Activity of Ribosome-Inactivating Proteins

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