Expression of the antimicrobial peptides in plants to control phytopathogenic bacteria and fungi

2006 ◽  
Vol 25 (6) ◽  
pp. 561-572 ◽  
Author(s):  
S. V. Oard ◽  
F. M. Enright
Keyword(s):  
Antimicrobial Peptides ◽  
Phytopathogenic Bacteria ◽  
Bacteria And Fungi

Antagonism against phytopathogenic bacteria and fungi and phytoregulating activity of streptomycetes of chernozems Moldova

2019 ◽  
Vol 326 (1) ◽  
pp. 131-136
Author(s):  
S.A. Burtseva ◽  
◽  
M.N. Byrsa ◽  
S.N. Maslobrod ◽  
◽  
...  
Keyword(s):  
Phytopathogenic Bacteria ◽  
Bacteria And Fungi

scholarly journals Plant antimicrobial peptides: structures, functions, and applications

2021 ◽  
Vol 62 (1) ◽  
Author(s):  
Junpeng Li ◽  
Shuping Hu ◽  
Wei Jian ◽  
Chengjian Xie ◽  
Xingyong Yang
Keyword(s):  
Antimicrobial Activity ◽  
Antimicrobial Peptides ◽  
Agricultural Production ◽  
Food Additives ◽  
Antimicrobial Activities ◽  
Gram Positive Bacteria ◽  
Potential Applications ◽  
Potential Applicability ◽  
Bacteria And Fungi ◽  
Positively Charged

AbstractAntimicrobial peptides (AMPs) are a class of short, usually positively charged polypeptides that exist in humans, animals, and plants. Considering the increasing number of drug-resistant pathogens, the antimicrobial activity of AMPs has attracted much attention. AMPs with broad-spectrum antimicrobial activity against many gram-positive bacteria, gram-negative bacteria, and fungi are an important defensive barrier against pathogens for many organisms. With continuing research, many other physiological functions of plant AMPs have been found in addition to their antimicrobial roles, such as regulating plant growth and development and treating many diseases with high efficacy. The potential applicability of plant AMPs in agricultural production, as food additives and disease treatments, has garnered much interest. This review focuses on the types of plant AMPs, their mechanisms of action, the parameters affecting the antimicrobial activities of AMPs, and their potential applications in agricultural production, the food industry, breeding industry, and medical field.

scholarly journals Antimicrobial activity of Paenibacillus peoriae strain NRRL BD-62 against a broad spectrum of phytopathogenic bacteria and fungi

2003 ◽  
Vol 95 (5) ◽  
pp. 1143-1151 ◽  
Author(s):  
I. Weid ◽  
D.S. Alviano ◽  
A.L.S. Santos ◽  
R.M.A. Soares ◽  
C.S. Alviano ◽  
...  
Keyword(s):  
Antimicrobial Activity ◽  
Broad Spectrum ◽  
Phytopathogenic Bacteria ◽  
Bacteria And Fungi

scholarly journals Synergy and remarkable specificity of antimicrobial peptides in vivo using a systematic knockout approach

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Mark Austin Hanson ◽  
Anna Dostálová ◽  
Camilla Ceroni ◽  
Mickael Poidevin ◽  
Shu Kondo ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Fungal Pathogens ◽  
Gene Editing ◽  
Cationic Peptides ◽  
Gram Negative Bacteria ◽  
Biological Processes ◽  
Gram Negative ◽  
Bacteria And Fungi

Antimicrobial peptides (AMPs) are host-encoded antibiotics that combat invading microorganisms. These short, cationic peptides have been implicated in many biological processes, primarily involving innate immunity. In vitro studies have shown AMPs kill bacteria and fungi at physiological concentrations, but little validation has been done in vivo. We utilized CRISPR gene editing to delete most known immune-inducible AMPs of Drosophila, namely: 4 Attacins, 2 Diptericins, Drosocin, Drosomycin, Metchnikowin and Defensin. Using individual and multiple knockouts, including flies lacking these ten AMP genes, we characterize the in vivo function of individual and groups of AMPs against diverse bacterial and fungal pathogens. We found that Drosophila AMPs act primarily against Gram-negative bacteria and fungi, contributing either additively or synergistically. We also describe remarkable specificity wherein certain AMPs contribute the bulk of microbicidal activity against specific pathogens, providing functional demonstrations of highly specific AMP-pathogen interactions in an in vivo setting.

scholarly journals Engineering of Marine-derived Antimicrobial Peptides (mAMPs) into Improved Anti-infective Drug Leads: A Mini-review

2021 ◽  
Vol 1192 (1) ◽  
pp. 012013
Author(s):  
L Sukmarini
Keyword(s):  
Antimicrobial Peptides ◽  
Chemical Diversity ◽  
Cytotoxic Activities ◽  
Small Molecular Weight ◽  
Resistance Development ◽  
Drug Candidates ◽  
Bacteria And Fungi ◽  
Drug Leads ◽  
Net Positive Charge

Abstract Marine-derived antimicrobial compounds possess chemical diversity varying from peptides, fatty acids to terpenes, alkaloids, and polyketides. These compounds, especially of peptide origin called antimicrobial peptides (AMPs), are present in the majority of marine organisms, including microbes (bacteria and fungi), invertebrates (molluscs, echinoderms, and sponges), vertebrates (fish and mammals), and plants (marine algae). They are defined by small molecular weight (less than 10 kDa), a net positive charge, and amphipathic structures. Moreover, due to their profound in vitro antimicrobial and cytotoxic activities and a low risk for resistance development, naturally occurring marine-derived AMPs (mAMPs) have been used as drug design templates for a large variety of semi-synthetic or synthetic AMPs, some of which have reached clinical trials. This mini-review aims to discuss AMPs from marine sources, mainly emphasizing the engineering of these peptides with improved pharmacological properties to develop drug candidates. Some selected recent examples of these engineered mAMPs as anti-infective drug leads are herein highlighted.

Structure-function relationships of antimicrobial peptides

1998 ◽  
Vol 76 (2-3) ◽  
pp. 235-246 ◽  
Author(s):  
Peter M Hwang ◽  
Hans J Vogel
Keyword(s):  
Antimicrobial Peptides ◽  
Hemolytic Activity ◽  
Mammalian Cells ◽  
Rational Design ◽  
Current Knowledge ◽  
Membrane Binding ◽  
Three Dimensional ◽  
Exact Nature ◽  
Additional Information ◽  
Bacteria And Fungi

Antimicrobial peptides are ubiquitously produced throughout nature. Many of these relatively short peptides (6-50 residues) are lethal towards bacteria and fungi, yet they display minimal toxicity towards mammalian cells. All of the peptides are highly cationic and hydrophobic. It is widely believed that they act through nonspecific binding to biological membranes, even though the exact nature of these interactions is presently unclear. High-resolution nuclear magnetic resonance (NMR) has contributed greatly to knowledge in this field, providing insight about peptide structure in aqueous solution, in organic cosolvents, and in micellar systems. Solid-state NMR can provide additional information about peptide-membrane binding. Here we review our current knowledge about the structure of antimicrobial peptides. We also discuss studies pertaining to the mechanism of action. Despite the different three-dimensional structural motifs of the various classes, they all have similar amphiphilic surfaces that are well-suited for membrane binding. Many antimicrobial peptides bind in a membrane-parallel orientation, interacting only with one face of the bilayer. This may be sufficient for antimicrobial action. At higher concentrations, peptides and phospholipids translocate to form multimeric transmembrane channels that seem to contribute to the peptide's hemolytic activity. An understanding of the key features of the secondary and tertiary structures of the antimicrobial peptides and their effects on bactericidal and hemolytic activity can aid the rational design of improved analogs for clinical use.Key words: structure, antimicrobial peptide, NMR, membrane, hemolytic.

scholarly journals Expression of an Antimicrobial Peptide via the Chloroplast Genome to Control Phytopathogenic Bacteria and Fungi

2001 ◽  
Vol 127 (3) ◽  
pp. 852-862 ◽  
Author(s):  
Gerald DeGray ◽  
Kanniah Rajasekaran ◽  
Franzine Smith ◽  
John Sanford ◽  
Henry Daniell
Keyword(s):  
Antimicrobial Peptide ◽  
Chloroplast Genome ◽  
Phytopathogenic Bacteria ◽  
Bacteria And Fungi

scholarly journals Synergy and remarkable specificity of antimicrobial peptides in vivo using a systematic knockout approach

2018 ◽  
Author(s):  
Mark Austin Hanson ◽  
Anna Dostalova ◽  
Camilla Ceroni ◽  
Mickael Poidevin ◽  
Shu Kondo ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Fungal Pathogens ◽  
Gene Editing ◽  
Cationic Peptides ◽  
Gram Negative Bacteria ◽  
Biological Processes ◽  
Gram Negative ◽  
Bacteria And Fungi

Antimicrobial peptides (AMPs) are host-encoded antibiotics that combat invading microorganisms. These short, cationic peptides have been implicated in many biological processes, primarily involving innate immunity. In vitro studies have shown AMPs kill bacteria and fungi at physiological concentrations, but little validation has been done in vivo. We utilised CRISPR gene editing to delete all known immune inducible AMPs of Drosophila, namely: 4 Attacins, 4 Cecropins, 2 Diptericins, Drosocin, Drosomycin, Metchnikowin and Defensin. Using individual and multiple knockouts, including flies lacking all 14 AMP genes, we characterize the in vivo function of individual and groups of AMPs against diverse bacterial and fungal pathogens. We found that Drosophila AMPs act primarily against Gram-negative bacteria and fungi, acting either additively or synergistically. We also describe remarkable specificity wherein certain AMPs contribute the bulk of microbicidal activity against specific pathogens, providing functional demonstrations of highly specific AMP-pathogen interactions in an in vivo setting.

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