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? (original) (raw)
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Biochimica et biophysica acta, 2018
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, li...
… et Biophysica Acta (BBA …, 1997
. The primary structure has been determined for PD-S2, a new type 1 ribosome-inactivating protein RIP , isolated from the seeds of Phytolacca dioica L. PD-S2 has 265 amino-acid residues, and a molecular mass of 29 586 Da. The polypeptide chain contains four amino-acid residues more than PAP-S, a type-1 RIP isolated from the seeds of the taxonomically related plant Phytolacca americana L. We have compared the amino-acid sequence of PD-S2 with those of two other RIPs with Ž . known three-dimensional structure: PAP-S and ricin A-chain RTA , the active chain of the best known type-2 RIP. This analysis shows an identity of 76% and 33% with PAP-S and RTA respectively, and a similarity of 82% and 54%.
Antibacterial Peptides from Plants: What They Are and How They Probably Work
Biochemistry Research International, 2011
Plant antibacterial peptides have been isolated from a wide variety of species. They consist of several protein groups with different features, such as the overall charge of the molecule, the content of disulphide bonds, and structural stability under environmental stress. Although the three-dimensional structures of several classes of plant peptides are well determined, the mechanism of action of some of these molecules is still not well defined. However, further studies may provide new evidences for their function on bacterial cell wall. Therefore, this paper focuses on plant peptides that show activity against plant-pathogenic and humanpathogenic bacteria. Furthermore, we describe the folding of several peptides and similarities among their three-dimensional structures. Some hypotheses for their mechanisms of action and attack on the bacterial membrane surface are also proposed.
Nature’s Antimicrobial Arsenal: Non-Ribosomal Peptides from PGPB for Plant Pathogen Biocontrol
Fermentation
Non-ribosomal peptides (NRPs) are a diverse group of bioactive compounds synthesized by microorganisms, and their antimicrobial properties make them ideal candidates for use as biocontrol agents against pathogens. Non-ribosomal peptides produced by Plant-Growth-Promoting Bacteria (PGPB) have gained interest for the biocontrol of plants’ bacterial and fungal pathogens. In this review, the structure and mode of action of NRPs, including their characterization and the characterization of NRP-producing microorganisms, are discussed. The use of NRPs in soilless agriculture and their potential as part of a sustainable plant disease control strategy are also highlighted. In addition, the review debates the commercial aspects of PGPB’s formulations and their potential as a biocontrol agent. Overall, this review emphasizes the importance of NRPs derived from PGPB in the biocontrol of plant pathogens and their potential to be used as an environmentally friendly and sustainable plant disease c...
Overview on Plant Antimicrobial Peptides
Mechanisms related to biotic interactions, such as pathogen attack, herbivory and symbiosisare important challenges to higher plants and have been widely studied especially for breeding purposes. The present review focuses on a special category of defense molecules, the plant antimicrobial peptides, providing an overview of their main molecular features and structures.
Antimicrobial peptides and plant disease control
FEMS Microbiology Letters, 2007
Several diseases caused by viruses, bacteria and fungi affect plant crops, resulting in losses and decreasing the quality and safety of agricultural products. Plant disease control relies mainly on chemical pesticides that are currently subject to strong restrictions and regulatory requirements. Antimicrobial peptides are interesting compounds in plant health because there is a need for new products in plant protection that fit into the new regulations. Living organisms secrete a wide range of antimicrobial peptides produced through ribosomal (defensins and small bacteriocins) or non-ribosomal synthesis (peptaibols, cyclopeptides and pseudopeptides). Several antimicrobial peptides are the basis for the design of new synthetic analogues, have been expressed in transgenic plants to confer disease protection or are secreted by microorganisms that are active ingredients of commercial biopesticides.
Host Defense Peptides and Their Potential as Therapeutic Agents, 2016
Disease afflicts crop productivity as well as nutritional attributes. Pathogens have the ability to mutate rapidly and thereby develop resistance to pesticides. Despite plant’s multilayer of innate defence against pathogens, often the latter are able to penetrate and establish themselves on plant host. The discovery of antimicrobial peptides (AMPs) has the promise of durable defence by quickly eliminating pathogens through membrane lysis. AMPs characteristically are made up of from fewer than 20 amino acids to about 100 amino acids, and yet are structurally diverse. AMPs in plants are classified into cyclotides, defensins, lipid transfer proteins (LTPs), thionins, snakins, hevein-like peptides, knottin-type peptides, and others. It is important to characterize and study mechanism of their action in order to develop a wide range of structures with the potential to provide durable plant immunity against pathogens. We bring together recent information on the mechanisms by which AMPs are able to help the plant to thwart pathogen attack. Although permeabilizing cellular membrane is a major mechanism known for AMP action, new and diverse modes of action have recently been unearthed, including targeting of intracellular function of the pathogen.
Scientific Reports, 2015
The recent increase in multidrug resistance against bacterial infections has become a major concern to human health and global food security. Synthetic antimicrobial peptides (AMPs) have recently received substantial attention as potential alternatives to conventional antibiotics because of their potent broad-spectrum antimicrobial activity. These peptides have also been implicated in plant disease control for replacing conventional treatment methods that are polluting and hazardous to the environment and to human health. Here, we report de novo design and antimicrobial studies of VG16, a 16-residue active fragment of Dengue virus fusion peptide. Our results reveal that VG16KRKP, a non-toxic and non-hemolytic analogue of VG16, shows significant antimicrobial activity against Gram-negative E. coli and plant pathogens X. oryzae and X. campestris, as well as against human fungal pathogens C. albicans and C. grubii. VG16KRKP is also capable of inhibiting bacterial disease progression in plants. The solution-NMR structure of VG16KRKP in lipopolysaccharide features a folded conformation with a centrally located turn-type structure stabilized by aromaticaromatic packing interactions with extended N-and C-termini. The de novo design of VG16KRKP provides valuable insights into the development of more potent antibacterial and antiendotoxic peptides for the treatment of human and plant infections. The remarkable increase in multi-drug resistance against conventional antibiotics observed in various pathogenic microorganisms has become one of the major concerns towards human health and global food security 1,2. Several Gram-negative bacterial strains are resistant towards multiple antibiotics and pose a great threat due to the absence of active bactericidal compounds 3,4. The use of antimicrobial peptides (AMPs) as novel antibiotics has been proposed and widely accepted for a long time. Due to their rapid and broad spectrum of antimicrobial properties along with their generalized mode of action, AMPs have been proposed for the treatment of microbial infections, specifically those caused by antibiotic-resistant bacteria 5-7. AMPs are generally small peptides having antimicrobial activity despite
Antimicrobial Peptides in Plants: Classes, Databases, and Importance
Canadian Journal of Biotechnology, 2019
Plant antimicrobial peptides (AMPs) are diverse molecules crucial in host defense mechanisms. These natural compounds display broad-spectrum antimicrobial activities and also play a significant role as immune modulators and anti-infective agents. They are classified into different families like defensins, thionins, cyclotides, snakins, and several others, based on the variation in their structure, the composition of amino acids, number of disulfide bonds, and mechanism of action. The ascending number of drugresistant plant and animal pathogens has pushed researchers to search for novel peptides, which can be utilized as alternatives to chemical antibiotics. In addition, the exhaustive genomic and proteomic data available on the cyberspace encourage the development of peptide libraries used for the prediction of unexplored peptides, thus saving time and cost for wet-lab experimentation. Understanding the insights of the structure and function of plant AMPs would offer excellent opportunities to expand their use as therapeutics in pharmaceutical and agricultural industries. This study reviewed the basis of plant AMPs, provided information on recent advancements in omic tools, and updated newly added peptides in the databases. The potential application of these peptides in human healthcare and agribusiness was also discussed.