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Novel bioactive peptides from PD-L1/2, a type 1 ribosome inactivating protein from Phytolacca dioica L. Evaluation of their antimicrobial properties and anti-biofilm activities.

Authors
  • Pizzo, Elio1
  • Pane, Katia1
  • Bosso, Andrea1
  • Landi, Nicola2
  • Ragucci, Sara2
  • Russo, Rosita2
  • Gaglione, Rosa3
  • Torres, Marcelo D T4
  • de la Fuente-Nunez, Cesar4
  • Arciello, Angela5
  • Di Donato, Alberto1
  • Notomista, Eugenio1
  • Di Maro, Antimo6
  • 1 Department of Biology, University of Naples 'Federico II', Via Cintia, I-80126 Napoli, Italy. , (Italy)
  • 2 Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', I-81100 Caserta, Italy. , (Italy)
  • 3 Department of Chemical Sciences, University of Naples 'Federico II' Via Cintia, I-80126 Napoli, Italy. , (Italy)
  • 4 Synthetic Biology Group, MIT Synthetic Biology Center, Massachusetts Institute of Technology, Cambridge, MA, United States.; Research Laboratory of Electronics, Massachusetts Institute of Technology, Cambridge, MA, United States.; Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA, United States.; Department of Electrical Engineering and Computer Science, Massachusetts Institute of Technology, Cambridge, MA, United States.; Broad Institute of MIT and Harvard, Cambridge, MA, United States.; Harvard Biophysics Program, Harvard University, Boston, MA, United States.; The Center for Microbiome Informatics and Therapeutics, Cambridge, MA, United States. , (United States)
  • 5 Department of Chemical Sciences, University of Naples 'Federico II' Via Cintia, I-80126 Napoli, Italy; Istituto Nazionale di Biostrutture e Biosistemi (INBB), Italy. , (Italy)
  • 6 Department of Environmental, Biological and Pharmaceutical Sciences and Technologies (DiSTABiF), University of Campania 'Luigi Vanvitelli', I-81100 Caserta, Italy. Electronic address: [email protected] , (Italy)
Type
Published Article
Journal
Biochimica et Biophysica Acta
Publisher
Elsevier
Publication Date
Apr 22, 2018
Volume
1860
Issue
7
Pages
1425–1435
Identifiers
DOI: 10.1016/j.bbamem.2018.04.010
PMID: 29684330
Source
Medline
Keywords
License
Unknown

Abstract

Antimicrobial peptides, also called Host Defence Peptides (HDPs), are effectors of innate immune response found in all living organisms. In a previous report, we have identified by chemical fragmentation, and characterized the first cryptic antimicrobial peptide in PD-L4, a type 1 ribosome inactivating protein (RIP) from leaves of Phytolacca dioica L. We applied a recently developed bioinformatic approach to a further member of the differently expressed pool of type 1 RIPs from P. dioica (PD-L1/2), and identified two novel putative cryptic HDPs in its N-terminal domain. These two peptides, here named IKY31 and IKY23, exhibit antibacterial activities against planktonic bacterial cells and, interestingly, significant anti-biofilm properties against two Gram-negative strains. Here, we describe that PD-L1/2 derived peptides are able to induce a strong dose-dependent reduction in biofilm biomass, affect biofilm thickness and, in the case of IKY31, interfere with cell-to-cell adhesion, likely by affecting biofilm structural components. In addition to these findings, we found that both PD-L1/2 derived peptides are able to assume stable helical conformations in the presence of membrane mimicking agents (SDS and TFE) and intriguingly beta structures when incubated with extracellular bacterial wall components (LPS and alginate). Overall, the data collected in this work provide further evidence of the importance of cryptic peptides derived from type 1 RIPs in host/pathogen interactions, especially under pathophysiological conditions induced by biofilm forming bacteria. This suggests a new possible role of RIPs as precursors of antimicrobial and anti-biofilm agents, likely released upon defensive proteolytic processes, which may be involved in plant homeostasis.

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