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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?
Author(s) -
Pizzo Elio,
Zanfardino Anna,
Di Giuseppe Antonella M.A.,
Bosso Andrea,
Landi Nicola,
Ragucci Sara,
Varcamonti Mario,
Notomista Eugenio,
Di Maro Antimo
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.08.018
Subject(s) - peptide , antimicrobial , antimicrobial peptides , biochemistry , ribosome inactivating protein , biology , fragmentation (computing) , chemistry , microbiology and biotechnology , ribosome , rna , gene , ecology
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.