Ribosome‐inactivating Proteins from Phytolaccaceae

Parente, Augusto; Maro, Antimo Di; Russo, Rosita; Severino, Valeria

doi:10.1002/9781118847237.ch3

Cited by 5 publications

(6 citation statements)

References 67 publications

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“…In order to verify if antimicrobial peptides similar to PDL4 40–65 are present in other type 1 RIPs from Phytolaccaceae [41] a multiple alignment with PD‐L4 was carried out ( Fig. S4).…”

Section: Resultsmentioning

confidence: 99%

A new active antimicrobial peptide from PD‐L4, a type 1 ribosome inactivating protein ofPhytolacca dioica L.: A new function of RIPs for plant defence?

et al. 2015

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a b s t r a c tWe investigated the antimicrobial activity of PD-L4, a type 1 RIP from Phytolacca dioica. We found that this protein is active on different bacterial strains both in a native and denatured/alkylated form and that this biological activity is related to a cryptic peptide, named PDL4 40-65 , identified by chemical fragmentation. This peptide showed the same antimicrobial activity of full-length protein and possessed, similarly to several antimicrobial peptides, an immunomodulatory effect on human cells. It assumes an alpha-helical conformation when interact with mimic membrane agents as TFE and likely bacterial membranes are a target of this peptide. To date PDL4 40-65 is the first antimicrobial peptide identified in a type 1 RIP.

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Section: Resultsmentioning

confidence: 99%

A new active antimicrobial peptide from PD‐L4, a type 1 ribosome inactivating protein ofPhytolacca dioica L.: A new function of RIPs for plant defence?

et al. 2015

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“…It has been reported that glycosylation can affect RIP activity. Protein synthesis inhibition activity of the recombinant PD-L1 (a type 1 RIP from P. dioica ) was increased after removal of the glycan chains [9]. In this study, the recombinant Md1RIP was synthesized following the secretory pathway for protein synthesis, though the native protein is most probably synthesized in the cytoplasm due to the lack of a signal peptide in the sequence.…”

Section: Discussionmentioning

confidence: 99%

“…Though multiple RIP sequences have been reported within one species, usually most of these sequences belong to the same class of RIP proteins. Several type 1 RIP isoforms have been reported in Phytolacca americana , referred to as pokeweed antiviral protein or PAP [9]. Different isoforms can occur within the same tissue and with differential expression during development.…”

Section: Introductionmentioning

confidence: 99%

Ribosome Inactivating Proteins from Rosaceae

2016

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Ribosome-inactivating proteins (RIPs) are widespread among higher plants of different taxonomic orders. In this study, we report on the RIP sequences found in the genome/transcriptome of several important Rosaceae species, including many economically important edible fruits such as apple, pear, peach, apricot, and strawberry. All RIP domains from Rosaceae share high sequence similarity with conserved residues in the catalytic site and the carbohydrate binding sites. The genomes of Malus domestica and Pyrus communis contain both type 1 and type 2 RIP sequences, whereas for Prunus mume, Prunus persica, Pyrus bretschneideri, and Pyrus communis a complex set of type 1 RIP sequences was retrieved. Heterologous expression and purification of the type 1 as well as the type 2 RIP from apple allowed to characterize the biological activity of the proteins. Both RIPs from Malus domestica can inhibit protein synthesis. Furthermore, molecular modelling suggests that RIPs from Rosaceae possess three-dimensional structures that are highly similar to the model proteins and can bind to RIP substrates. Screening of the recombinant type 2 RIP from apple on a glycan array revealed that this type 2 RIP interacts with terminal sialic acid residues. Our data suggest that the RIPs from Rosaceae are biologically active proteins.

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“…The fact that PD-L4 does not show antifungal activity [ 30 ] despite showing high homology with PD-S2 [ 113 ] suggests that entry into cells may be the limiting step for the fungicidal capacity of RIPs, and it has been suggested that the amphipathicity of the carboxyl-terminal domain could play a relevant role in the different degrees of toxicity of RIPs towards fungi [ 30 ]. In fact, BE27, which is the most toxic to P. digitatum , is the one with the highest degree of amphipathicity in the carboxyl-terminal domain and has been shown to be able to internalize and depurinate fungal ribosomes [ 29 ].…”

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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Ribosome‐inactivating Proteins from Phytolaccaceae

Cited by 5 publications

References 67 publications

A new active antimicrobial peptide from PD‐L4, a type 1 ribosome inactivating protein ofPhytolacca dioica L.: A new function of RIPs for plant defence?

A new active antimicrobial peptide from PD‐L4, a type 1 ribosome inactivating protein ofPhytolacca dioica L.: A new function of RIPs for plant defence?

Ribosome Inactivating Proteins from Rosaceae

Antifungal Activity of Ribosome-Inactivating Proteins

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