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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?
- Source :
-
FEBS letters [FEBS Lett] 2015 Sep 14; Vol. 589 (19 Pt B), pp. 2812-8. Date of Electronic Publication: 2015 Aug 20. - Publication Year :
- 2015
-
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.<br /> (Copyright © 2015 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)
- Subjects :
- Amino Acid Sequence
Anti-Infective Agents chemistry
Anti-Infective Agents toxicity
Bacteria drug effects
Caco-2 Cells
Humans
Molecular Sequence Data
Peptide Fragments chemistry
Peptide Fragments toxicity
Phytolacca chemistry
Plant Leaves chemistry
Plant Proteins chemistry
Protein Conformation
Ribosome Inactivating Proteins chemistry
Anti-Infective Agents pharmacology
Peptide Fragments pharmacology
Phytolacca physiology
Plant Proteins metabolism
Ribosome Inactivating Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1873-3468
- Volume :
- 589
- Issue :
- 19 Pt B
- Database :
- MEDLINE
- Journal :
- FEBS letters
- Publication Type :
- Academic Journal
- Accession number :
- 26297825
- Full Text :
- https://doi.org/10.1016/j.febslet.2015.08.018