Apidaecin-type peptides: Biodiversity, structure–function relationships and mode of action

Antimicrobial peptides

“…Undesirably, application of AMPs to engineer pathogen resistance in plants suffers from some limitations, namely species-and race-specificity of the peptides, 120 slight enhanced resistance, 106 induction of infertility, 121 and leakage of conferred resistance after a while due to resiliency of disease-causing microbes. 38 To alleviate these drawbacks as well as to increase the antimicrobial potency of existing peptides, several approaches have been proposed to follow. Engineering crop plants for disease resistance via chloroplast genome instead of nuclear genome is proposed to achieve high levels of expression and to prevent pollen-mediated escape of transgenes.…”

“…40 Peptides self-associate onto the acidic phospholipid-rich regions of lipid bilayers and once their concentrations reach a certain threshold they permeate into the membrane by mounting the bilayer positive potential. 38 The second pore-formation mechanism "barrel-stave" 63 is symbolized in alamethicin; 60 it inserts into the membrane hydrophobic area and creates a pore by forming trans-membrane helical bundles. In the third mechanism, the "toroidal" model, the peptide builds toroidal pores in lipid bilayers.…”

“…They are lethal to many Gram-negative bacteria. 38 Of interest, several linear AMPs are amorphous in free solution and fold into their final configuration upon partitioning into biological membranes. …”

“…Nevertheless, apidaecins belonging to short Pro-rich peptides are of distinction by lacking the pore-inducing action. 38 Eradication of bacteria by apidaecins commences by an ambiguous interaction of the peptide with an outer membrane component like LPS and DnaK, 68 and consequently, its entrance into the periplasmic space. Next, peptide traverses inner membrane specifically by an irrevocable band with either a receptor/docking/transporter molecule 69 or the 60-kDa bacterial chaperone GroEL.…”

Interaction of Apidaecin Ib with Phospholipid Bilayers and its Edwardsiella Species-specific Antimicrobial Activity

“…[7][8][9] In this regard, apidaecin-like peptides have recently been considered as a good candidate for the new alternatives against fish Gram-negative bacteria such as Aeromonas spp., Edwardsiella spp., and Vibrio spp. Although apidaecins have been applied recently as feed additives instead of antibiotics for common carp basal ditets for investigation of its effectiveness on growth performances and immune function, there is no report for the screening of antibacterial activity of apidaecins against specific fish pathogenic bacteria, espicially Edwardsiella species.…”