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

2015; Wiley; Volume: 589; Issue: 19PartB Linguagem: Inglês

10.1016/j.febslet.2015.08.018

1873-3468

Elio Pizzo, Anna Zanfardino, Antonella M.A. Di Giuseppe, Andrea Bosso, Nicola Landi, Sara Ragucci, Mario Varcamonti, Eugenio Notomista, Antimo Di Maro,

Biochemical and Structural Characterization

We 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.