Spermicidal efficacy of VRP, a synthetic cationic antimicrobial peptide, inducing apoptosis and membrane disruption

2017 ◽  
Vol 233 (2) ◽  
pp. 1041-1050 ◽  
Author(s):  
Prasanta Ghosh ◽  
Arpita Bhoumik ◽  
Sudipta Saha ◽  
Sandipan Mukherjee ◽  
Sarfuddin Azmi ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Membrane Disruption ◽  
Cationic Antimicrobial Peptide

Acyl carrier protein is a bacterial cytoplasmic target of cationic antimicrobial peptide LL-37

2015 ◽  
Vol 470 (2) ◽  
pp. 243-253 ◽  
Author(s):  
Myung-Chul Chung ◽  
Scott N. Dean ◽  
Monique L. van Hoek
Keyword(s):  
Antimicrobial Peptide ◽  
Acyl Carrier Protein ◽  
Acid Synthesis ◽  
Membrane Disruption ◽  
Carrier Protein ◽  
Cytoplasmic Protein ◽  
Bacterial Killing ◽  
Cationic Antimicrobial Peptide ◽  
Antibiotic Resistant ◽  
Future Drug

In addition to membrane disruption, the cathelicidin antimicrobial peptide LL-37 translocates through the bacterial inner membrane to target intracellular molecules. Our data suggest that the CAMP LL-37 is able can specifically bind to the cytoplasmic protein AcpP resulting in the inhibition of fatty acid synthesis and bacterial killing. Our studies introduce a novel mechanism for cationic antimicrobial peptides, which may be useful in future drug development for the treatment of antibiotic-resistant bacterial infection.

scholarly journals Phage-encoded cationic antimicrobial peptide used for outer membrane disruption in lysis

2019 ◽  
Author(s):  
Ashley Holt ◽  
Jesse Cahill ◽  
Jolene Ramsey ◽  
Chandler O’Leary ◽  
Russell Moreland ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Antimicrobial Peptide ◽  
Outer Membrane ◽  
Genetic Selection ◽  
Helical Structure ◽  
Bioinformatic Analysis ◽  
Membrane Disruption ◽  
Bacterial Cells ◽  
New Paradigm ◽  
Cationic Antimicrobial Peptide

AbstractSpanins are required for the last step in bacteriophage lysis: the disruption of the outer membrane. Bioinformatic analysis has shown that ~15% of phages lack a spanin gene, which suggests an alternate mechanism of outer membrane disruption. To address this, we selected virulent podophage ϕKT as a spaninless exemplar and tested ϕKT genes for outer membrane disruption during lysis. Hypothetical novel gene 28 causes outer membrane disruption when co-expressed with ϕKT lysis genes and complements the lysis defect of a λ spanin mutant. Gp28 is a 56 aa cationic peptide with predicted amphipathic helical structure and is associated with the particulate fraction after lysis. Urea and KCl washes did not release gp28 from the particulate, suggesting a strong hydrophobic interaction with the membrane. Super high-resolution microscopy supports a primarily outer membrane localization for the peptide. Additionally, holin function is not required for gp28-mediated lysis. Gp28 is similar in size, charge, predicted fold, and membrane association to the human cathelicidin antimicrobial peptide LL-37. In standard assays to measure bactericidal and inhibitory effects of antimicrobial peptides on bacterial cells, synthesized gp28 performed equivalently to LL-37. The studies presented here suggest that ϕKT Gp28 disrupts bacterial outer membranes during lysis in a manner akin to antimicrobial peptides.SignificanceHere we provide evidence that ϕKT produces an antimicrobial peptide for outer membrane disruption during lysis. The disruptin is a new paradigm for phage lysis, and has no similarities to other known lysis genes. Many mechanisms have been proposed for the function of antimicrobial peptides, however there is not a consensus on the molecular basis of membrane disruption. Additionally, there is no established genetic selection system to support such studies. Therefore, the ϕKT disruptin may represent the first genetically tractable antimicrobial peptide.

Phage-encoded cationic antimicrobial peptide required for lysis

2021 ◽  
Author(s):  
Ashley Holt ◽  
Jesse Cahill ◽  
Jolene Ramsey ◽  
Cody Martin ◽  
Chandler O’Leary ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Outer Membrane ◽  
Genetic System ◽  
Membrane Disruption ◽  
New Paradigm ◽  
Hydrophobic Membrane ◽  
Cationic Protein ◽  
Cationic Antimicrobial Peptide ◽  
Host Lysis ◽  
K 12

Most phages of Gram-negative hosts encode spanins for disruption of the outer membrane, the last step in host lysis. However, bioinformatic analysis indicates that ∼15% of these phages lack a spanin gene, suggesting they have an alternate way of disrupting the OM. Here, we show that the T7-like coliphage phiKT causes the explosive cell lysis associated with spanin activity despite not encoding spanins. A putative lysis cassette cloned from the phiKT late gene region includes the hypothetical novel gene 28 located between the holin and endolysin genes and supports inducible lysis in E. coli K-12. Moreover, induction of an isogenic construct lacking gene 28 resulted in divalent cation-stabilized spherical cells rather than lysis, implicating gp 28 in OM disruption. Additionally, gp 28 was shown to complement the lysis defect of a spanin-null λ lysogen. Gene 28 encodes a 56-amino acid cationic protein with predicted amphipathic helical structure and is membrane-associated after lysis. Urea and KCl washes did not release gp 28 from the particulate, suggesting a strong hydrophobic membrane interaction. Fluorescence microscopy supports membrane localization of the gp 28 protein prior to lysis. Gp 28 is similar in size, charge, predicted fold, and membrane association to the human cathelicidin antimicrobial peptide LL-37. Synthesized gp 28 behaved similar to LL-37 in standard assays mixing peptide and cells to measure bactericidal and inhibitory effects. Taken together, these results indicate that phiKT gp 28 is a phage-encoded cationic antimicrobial peptide that disrupts bacterial outer membranes during host lysis and thus establishes a new class of phage lysis proteins, the disruptins. Significance We provide evidence that phiKT produces an antimicrobial peptide for outer membrane disruption during lysis. This protein, designated as a disruptin, is a new paradigm for phage lysis and has no similarities to other known lysis genes. Although many mechanisms have been proposed for the function of antimicrobial peptides, there is no consensus on the molecular basis of membrane disruption. Additionally, there is no established genetic system to support such studies. Therefore, the phiKT disruptin may represent the first genetically tractable antimicrobial peptide, facilitating mechanistic analyses.

scholarly journals Helical cationic antimicrobial peptide length and its impact on membrane disruption

2015 ◽  
Vol 1848 (5) ◽  
pp. 1081-1091 ◽  
Author(s):  
Melanie L. Juba ◽  
Devin K. Porter ◽  
Elissa H. Williams ◽  
Carlos A. Rodriguez ◽  
Stephanie M. Barksdale ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Membrane Disruption ◽  
Cationic Antimicrobial Peptide ◽  
Peptide Length

Highly efficient nanomedicine from cationic antimicrobial peptide-protected Ag nanoclusters

2021 ◽  
Author(s):  
Zhikai Ye ◽  
Haishuang Zhu ◽  
Shan Zhang ◽  
Jing Li ◽  
Jin Wang ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Biological Systems ◽  
Cationic Antimicrobial Peptide ◽  
Highly Efficient ◽  
Antimicrobial Efficiency ◽  
Ag Nanoclusters ◽  
Fine Tune

Designing the homogeneous assembly of the bio–nano interface to fine-tune the interactions between the nanoprobes and biological systems is of prime importance to improve the antimicrobial efficiency of nanomedicines.

scholarly journals Insights into the Action Mechanism of the Antimicrobial Peptide Lasioglossin III

2021 ◽  
Vol 22 (6) ◽  
pp. 2857
Author(s):  
Filomena Battista ◽  
Rosario Oliva ◽  
Pompea Del Vecchio ◽  
Roland Winter ◽  
Luigi Petraccone
Keyword(s):  
Antimicrobial Peptide ◽  
Gram Negative Bacteria ◽  
Lipid Domains ◽  
Action Mechanism ◽  
Cationic Antimicrobial Peptide ◽  
Intracellular Targeting ◽  
Gel Retardation Assay ◽  
Charged Membrane ◽  
Intracellular Target ◽  
Anionic Lipids

Lasioglossin III (LL-III) is a cationic antimicrobial peptide derived from the venom of the eusocial bee Lasioglossum laticeps. LL-III is extremely toxic to both Gram-positive and Gram-negative bacteria, and it exhibits antifungal as well as antitumor activity. Moreover, it shows low hemolytic activity, and it has almost no toxic effects on eukaryotic cells. However, the molecular basis of the LL-III mechanism of action is still unclear. In this study, we characterized by means of calorimetric (DSC) and spectroscopic (CD, fluorescence) techniques its interaction with liposomes composed of a mixture of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) and 1-palmitoyl-2-oleoyl-sn-glycero-3-rac-phosphoglycerol (POPG) lipids as a model of the negatively charged membrane of pathogens. For comparison, the interaction of LL-III with the uncharged POPC liposomes was also studied. Our data showed that LL-III preferentially interacted with anionic lipids in the POPC/POPG liposomes and induces the formation of lipid domains. Furthermore, the leakage experiments showed that the peptide could permeabilize the membrane. Interestingly, our DSC results showed that the peptide-membrane interaction occurs in a non-disruptive manner, indicating an intracellular targeting mode of action for this peptide. Consistent with this hypothesis, our gel-retardation assay experiments showed that LL-III could interact with plasmid DNA, suggesting a possible intracellular target.

scholarly journals Encapsulation of a cationic antimicrobial peptide into self-assembled polyion complex nano-objects enhances its antitumor properties

2022 ◽  
Vol 1249 ◽  
pp. 131482
Author(s):  
Mina Răileanu ◽  
Barbara Lonetti ◽  
Charles-Louis Serpentini ◽  
Dominique Goudounèche ◽  
Laure Gibot ◽  
...  
Keyword(s):  
Antimicrobial Peptide ◽  
Cationic Antimicrobial Peptide ◽  
Polyion Complex ◽  
Antitumor Properties ◽  
Self Assembled

Cationic antimicrobial peptide and its poly-N-substituted glycine congener: Antibacterial and antibiofilm potential against A. baumannii

2019 ◽  
Vol 518 (3) ◽  
pp. 472-478 ◽  
Author(s):  
Deepika Sharma ◽  
Monika Choudhary ◽  
Jitendraa Vashistt ◽  
Rahul Shrivastava ◽  
Gopal Singh Bisht
Keyword(s):  
Antimicrobial Peptide ◽  
Cationic Antimicrobial Peptide
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