Mode of action of diptericin A, a bactericidal peptide induced in the hemolymph of <i>Phormia terranovae</i> larvae

Keppi, Elisabeth; Pugsley, Anthony P.; Lambert, Jean; Wicker, Claude; Dimarcq, Jean‐Luc; Hoffmann, Jules A.; Hoffmann, D.

doi:10.1002/arch.940100306

Cited by 26 publications

(20 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…While proline‐ and glycine‐rich peptides such as diptericin are predominantly active against Gram‐negative bacteria (Keppi et al ., 1989), prolixicin, like cecropins, is active against both Gram‐positive and Gram‐negative bacteria (Moore et al ., 1996). In addition to their antibacterial properties, proline‐rich peptides have been evaluated for antiparasite activity.…”

Section: Discussionmentioning

confidence: 66%

Prolixicin: a novel antimicrobial peptide isolated from Rhodnius prolixus with differential activity against bacteria and Trypanosoma cruzi

Ursic-Bedoya

Buchhop

Joy

et al. 2011

Insect Molecular Biology

View full text Add to dashboard Cite

We identified and characterized the activity of prolixicin, a novel antimicrobial peptide (AMP) isolated from the hemipteran insect, Rhodnius prolixus. Sequence analysis reveals one region of prolixicin that may be related to the diptericin/attacin family of AMPs. Prolixicin is an 11-kDa peptide containing a putative 21 amino acid signal peptide, two putative phosphorylation sites and no glycosylation sites. It is produced by both adult fat body and midgut tissues in response to bacterial infection of the haemolymph or the midgut. Unlike most insect antibacterial peptides, the prolixicin gene does not seem to be regulated by NF-κB binding sites, but its promoter region contains several GATA sites. Recombinant prolixicin has strong activity against the Gram-negative bacterium Escherichia coli and differential activity against several Gram-negative and Gram-positive bacteria. No significant toxicity was demonstrated against Trypanosoma cruzi, the human parasite transmitted by R. prolixus.

show abstract

Section: Discussionmentioning

confidence: 66%

Prolixicin: a novel antimicrobial peptide isolated from Rhodnius prolixus with differential activity against bacteria and Trypanosoma cruzi

Ursic-Bedoya

Buchhop

Joy

et al. 2011

Insect Molecular Biology

View full text Add to dashboard Cite

show abstract

“…Surprisingly, no activity was detected against yeasts of the Candida genus. Indeed, glycine-rich peptides are generally reported to be active against Gram-negative bacteria and/or fungi (including yeasts) as it was described for arthropod AMPs like acanthoscurrins ( Lorenzini et al, 2003 ), coleoptericin ( Bulet et al, 1991 ), ctenidins ( Baumann et al, 2010 ), diptericin A ( Keppi et al, 1989 ), holotricin 3 ( Lee et al, 1995 ), or tenecin 3 ( Lee et al, 1996 ), frog AMPs like leptoglycin ( Sousa et al, 2009 ) and plant AMPs like shepherins ( Park et al, 2000 ) ( Table 3 ). However, some exceptions exist like hyastatin from the spider crab Hyas araneus that exhibits a broad spectrum of antimicrobial activity ( Sperstad et al, 2009 ), or SK84 from Drosophila virilis that appears to be only active against Gram-positive bacteria ( Lu and Chen, 2010 ).…”

Section: Discussionmentioning

confidence: 97%

Armadillidin H, a Glycine-Rich Peptide from the Terrestrial Crustacean Armadillidium vulgare, Displays an Unexpected Wide Antimicrobial Spectrum with Membranolytic Activity

et al. 2016

View full text Add to dashboard Cite

Antimicrobial peptides (AMPs) are key components of innate immunity and are widespread in nature, from bacteria to vertebrate animals. In crustaceans, there are currently 15 distinct AMP families published so far in the literature, mainly isolated from members of the Decapoda order. Up to now, armadillidin is the sole non-decapod AMP isolated from the haemocytes of Armadillidium vulgare, a crustacean isopod. Its first description demonstrated that armadillidin is a linear glycine-rich (47%) cationic peptide with an antimicrobial activity directed toward Bacillus megaterium. In the present work, we report identification of armadillidin Q, a variant of armadillidin H (earlier known as armadillidin), from crude haemocyte extracts of A. vulgare using LC-MS approach. We demonstrated that both armadillidins displayed broad spectrum antimicrobial activity against several Gram-positive and Gram-negative bacteria, fungi, but were totally inactive against yeasts. Membrane permeabilization assays, only performed with armadillidin H, showed that the peptide is membrane active against bacterial and fungal strains leading to deep changes in cell morphology. This damaging activity visualized by electronic microscopy correlates with a rapid decrease of cell viability leading to highly blebbed cells. In contrast, armadillidin H does not reveal cytotoxicity toward human erythrocytes. Furthermore, no secondary structure could be defined in this study [by circular dichroism (CD) and nuclear magnetic resonance (NMR)] even in a membrane mimicking environment. Therefore, armadillidins represent interesting candidates to gain insight into the biology of glycine-rich AMPs.

show abstract

“…Calliphora diptericins are members of a glycine-rich AMP family selectively toxic to some Gram-negative Enterobacteria like E . coli by means of cell wall disruption [ 35 ]. Calliphora proline-rich peptides belong to the family of proline/arginine-rich AMPs.…”

Section: Discussionmentioning

confidence: 99%

Insect Antimicrobial Peptide Complexes Prevent Resistance Development in Bacteria

2015

View full text Add to dashboard Cite

In recent decades much attention has been paid to antimicrobial peptides (AMPs) as natural antibiotics, which are presumably protected from resistance development in bacteria. However, experimental evolution studies have revealed prompt resistance increase in bacteria to any individual AMP tested. Here we demonstrate that naturally occurring compounds containing insect AMP complexes have clear advantage over individual peptide and small molecule antibiotics in respect of drug resistance development. As a model we have used the compounds isolated from bacteria challenged maggots of Calliphoridae flies. The compound isolated from blow fly Calliphora vicina was found to contain three distinct families of cell membrane disrupting/permeabilizing peptides (defensins, cecropins and diptericins), one family of proline rich peptides and several unknown antimicrobial substances. Resistance changes under long term selective pressure of the compound and reference antibiotics cefotaxime, meropenem and polymyxin B were tested using Escherichia coli, Klebsiella pneumonia and Acinetobacter baumannii clinical strains. All the strains readily developed resistance to the reference antibiotics, while no signs of resistance growth to the compound were registered. Similar results were obtained with the compounds isolated from 3 other fly species. The experiments revealed that natural compounds containing insect AMP complexes, in contrast to individual AMP and small molecule antibiotics, are well protected from resistance development in bacteria. Further progress in the research of natural AMP complexes may provide novel solutions to the drug resistance problem.

show abstract

Mode of action of diptericin A, a bactericidal peptide induced in the hemolymph of Phormia terranovae larvae

Cited by 26 publications

References 21 publications

Prolixicin: a novel antimicrobial peptide isolated from Rhodnius prolixus with differential activity against bacteria and Trypanosoma cruzi

Prolixicin: a novel antimicrobial peptide isolated from Rhodnius prolixus with differential activity against bacteria and Trypanosoma cruzi

Armadillidin H, a Glycine-Rich Peptide from the Terrestrial Crustacean Armadillidium vulgare, Displays an Unexpected Wide Antimicrobial Spectrum with Membranolytic Activity

Insect Antimicrobial Peptide Complexes Prevent Resistance Development in Bacteria

Contact Info

Product

Resources

About