title: 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?
abstract: 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 PDL440-65, 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 PDL440-65 is the first antimicrobial peptide identified in a type 1 RIP.
authors: Department of Biology, University of Naples "Federico II" Via Cintia, I-80126 Napoli, Italy. Electronic address: eliodoro.pizzo@unina.it.
authors: Elio
authors: E
authors: Pizzo
authors: Department of Biology, University of Naples "Federico II" Via Cintia, I-80126 Napoli, Italy.
authors: Anna
authors: A
authors: Zanfardino
authors: Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, Second University of Naples, I-81100 Caserta, Italy.
authors: Antonella M A
authors: AM
authors: Di Giuseppe
authors: Department of Biology, University of Naples "Federico II" Via Cintia, I-80126 Napoli, Italy.
authors: Andrea
authors: A
authors: Bosso
authors: Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, Second University of Naples, I-81100 Caserta, Italy.
authors: Nicola
authors: N
authors: Landi
authors: Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, Second University of Naples, I-81100 Caserta, Italy.
authors: Sara
authors: S
authors: Ragucci
authors: Department of Biology, University of Naples "Federico II" Via Cintia, I-80126 Napoli, Italy.
authors: Mario
authors: M
authors: Varcamonti
authors: Department of Biology, University of Naples "Federico II" Via Cintia, I-80126 Napoli, Italy.
authors: Eugenio
authors: E
authors: Notomista
authors: Department of Environmental, Biological and Pharmaceutical Sciences and Technologies, Second University of Naples, I-81100 Caserta, Italy. Electronic address: antimo.dimaro@unina2.it.
authors: Antimo
authors: A
authors: Di Maro
mesh_terms: D000595:Amino Acid Sequence; D000890:Anti-Infective Agents / Q000737:chemistry / Q000494:pharmacology* / Q000633:toxicity; D001419:Bacteria / Q000187:drug effects; D018938:Caco-2 Cells; D006801:Humans; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000737:chemistry / Q000494:pharmacology* / Q000633:toxicity; D029603:Phytolacca / Q000737:chemistry / Q000502:physiology*; D018515:Plant Leaves / Q000737:chemistry; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D054788:Ribosome Inactivating Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D000890:Anti-Infective Agents; D010446:Peptide Fragments; D010940:Plant Proteins; D054788:Ribosome Inactivating Proteins
keywords: Antimicrobial peptide; Cationic antimicrobial peptide; Phytolacca dioica; Ribosome inactivating protein