scholarly journals Pseudonajide is an antibiotic peptide derived from snake venom that alter cell wall and membrane integrity interfering on biofilm formation.

2019 ◽  
Author(s):  
Rafael Schneider ◽  
Muriel Primon-Barros ◽  
Rafael Gomes Von Borowski ◽  
Sophie Chat ◽  
Reynald Gillet ◽  
...  
Keyword(s):  
Cell Wall ◽  
Snake Venom ◽  
Biofilm Formation ◽  
Bacterial Resistance ◽  
Cell Damage ◽  
Cell Envelope ◽  
Membrane Integrity ◽  
Antibiofilm Activity ◽  
Sequence Alignments ◽  
Resistance Phenotype

Abstract Background The increase of bacterial resistance phenotype cases is a global health problem. New strategies in scientific community must be explored in order to create new treatment alternatives. Animal venoms are a good source for antimicrobial peptides (AMPs), which are excellent candidates for new antimicrobial drug development. These molecules have highly diverse targets in prokaryotic cells, making resistance phenotype development more difficult. Results In this study we present a peptide of just 11 amino acids which has antimicrobial and antibiofilm activity against Staphyloccocus epidermidis. Named pseudonajide, it is derived from Pseudonaja textilis venom. Pseudonajide was selected based on the sequence alignments of various snake venom peptides that displayed activity against bacteria. Several concentrations of pseudonajide were tested in antibiofilm activity essay, it was detected that 25 µM was the best minimal concentration for biofilm inhibiting activity. Microscopy analysis demonstrates that pseudonajide interacts with the bacterial cell envelope, disrupting the cell wall and membrane leading to morphological defects in prokaryotes. Conclusions Our results suggest that pseudonajide’s positives charges interacts with negative charged cell wall components of S. epidermidis. Leading to cell damage and biofilm formation inhibition.

scholarly journals Pseudonajide peptide derived from snake venom alters cell envelope integrity interfering on biofilm formation in Staphylococcus epidermidis

2020 ◽  
Author(s):  
Rafael Schneider ◽  
Muriel Primon-Barros ◽  
Rafael Gomes Von Borowski ◽  
Sophie Chat ◽  
Sylvie Nonin-Lecomte ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Snake Venom ◽  
Staphylococcus Epidermidis ◽  
Biofilm Formation ◽  
Bacterial Infections ◽  
Bacterial Resistance ◽  
Cell Damage ◽  
Cell Envelope ◽  
Antibiofilm Activity ◽  
Sequence Alignments

Abstract Background The increase in bacterial resistance phenotype cases is a global health problem. New strategies must be explored by the scientific community in order to create new treatment alternatives. Animal venoms are a good source for antimicrobial peptides (AMPs), which are excellent candidates for new antimicrobial drug development. Cathelicidin-related antimicrobial peptides (CRAMPs) from snake venoms have been studied as a model for the design of new antimicrobial pharmaceuticals against bacterial infections. Results In this study we present an 11 amino acid-long peptide, named pseudonajide, which is derived from a Pseudonaja textilis venom peptide and has antimicrobial and antibiofilm activity against Staphylococcus epidermidis . Pseudonajide was selected based on the sequence alignments of various snake venom peptides that displayed activity against bacteria. Antibiofilm activity assays with pseudonajide concentrations ranging from 3.12 to 100 µM showed that the lowest concentration to inhibit biofilm formation was 25 µM. Microscopy analysis demonstrated that pseudonajide interacts with the bacterial cell envelope, disrupting the cell walls and membranes, leading to morphological defects in prokaryotes. Conclusions Our results suggest that pseudonajide’s positives charges interact with negatively charged cell wall components of S. epidermidis, leading to cell damage and inhibiting biofilm formation.

scholarly journals Pseudonajide peptide derived from snake venom alters cell envelope integrity interfering on biofilm formation in Staphylococcus epidermidis

2020 ◽  
Author(s):  
Rafael Schneider ◽  
Muriel Primon-Barros ◽  
Rafael Gomes Von Borowski ◽  
Sophie Chat ◽  
Sylvie Nonin-Lecomte ◽  
...  
Keyword(s):  
Antimicrobial Peptides ◽  
Snake Venom ◽  
Staphylococcus Epidermidis ◽  
Biofilm Formation ◽  
Bacterial Infections ◽  
Bacterial Resistance ◽  
Cell Damage ◽  
Cell Envelope ◽  
Antibiofilm Activity ◽  
Sequence Alignments

Abstract Background The increase in bacterial resistance phenotype cases is a global health problem. New strategies must be explored by the scientific community in order to create new treatment alternatives. Animal venoms are a good source for antimicrobial peptides (AMPs), which are excellent candidates for new antimicrobial drug development. Cathelicidin-related antimicrobial peptides (CRAMPs) from snake venoms have been studied as a model for the design of new antimicrobial pharmaceuticals against bacterial infections. Results In this study we present an 11 amino acid-long peptide, named pseudonajide, which is derived from a Pseudonaja textilis venom peptide and has antimicrobial and antibiofilm activity against Staphylococcus epidermidis . Pseudonajide was selected based on the sequence alignments of various snake venom peptides that displayed activity against bacteria. Antibiofilm activity assays with pseudonajide concentrations ranging from 3.12 to 100 µM showed that the lowest concentration to inhibit biofilm formation was 25 µM. Microscopy analysis demonstrated that pseudonajide interacts with the bacterial cell envelope, disrupting the cell walls and membranes, leading to morphological defects in prokaryotes. Conclusions Our results suggest that pseudonajide’s positives charges interact with negatively charged cell wall components of S. epidermidis, leading to cell damage and inhibiting biofilm formation.

scholarly journals Pseudonajide peptide derived from snake venom alters cell envelope integrity interfering on biofilm formation in Staphylococcus epidermidis

2020 ◽  
Vol 20 (1) ◽  
Author(s):  
Rafael Schneider ◽  
Muriel Primon-Barros ◽  
Rafael Gomes Von Borowski ◽  
Sophie Chat ◽  
Sylvie Nonin-Lecomte ◽  
...  
Keyword(s):  
Snake Venom ◽  
Staphylococcus Epidermidis ◽  
Biofilm Formation ◽  
Cell Envelope

scholarly journals Antimicrobial and Antibiofilm Peptides

Biomolecules ◽  
2020 ◽  
Vol 10 (4) ◽  
pp. 652 ◽  
Author(s):  
Angela Di Somma ◽  
Antonio Moretta ◽  
Carolina Canè ◽  
Arianna Cirillo ◽  
Angela Duilio
Keyword(s):  
Antimicrobial Peptides ◽  
Biofilm Formation ◽  
Bacterial Resistance ◽  
Antimicrobial Agents ◽  
Multidrug Resistant ◽  
Resistant Bacteria ◽  
Antibiofilm Activity ◽  
Chronic Infections ◽  
Planktonic Bacteria ◽  
Hostile Environments

The increasing onset of multidrug-resistant bacteria has propelled microbiology research towards antimicrobial peptides as new possible antibiotics from natural sources. Antimicrobial peptides are short peptides endowed with a broad range of activity against both Gram-positive and Gram-negative bacteria and are less prone to trigger resistance. Besides their activity against planktonic bacteria, many antimicrobial peptides also show antibiofilm activity. Biofilms are ubiquitous in nature, having the ability to adhere to virtually any surface, either biotic or abiotic, including medical devices, causing chronic infections that are difficult to eradicate. The biofilm matrix protects bacteria from hostile environments, thus contributing to the bacterial resistance to antimicrobial agents. Biofilms are very difficult to treat, with options restricted to the use of large doses of antibiotics or the removal of the infected device. Antimicrobial peptides could represent good candidates to develop new antibiofilm drugs as they can act at different stages of biofilm formation, on disparate molecular targets and with various mechanisms of action. These include inhibition of biofilm formation and adhesion, downregulation of quorum sensing factors, and disruption of the pre-formed biofilm. This review focuses on the proprieties of antimicrobial and antibiofilm peptides, with a particular emphasis on their mechanism of action, reporting several examples of peptides that over time have been shown to have activity against biofilm.

scholarly journals Antibiofilm Activity of Acidic Phospholipase Isoform Isolated from Bothrops erythromelas Snake Venom

2020 ◽  
Author(s):  
Ellynes Nunes ◽  
Breno Frihling ◽  
Elizângela Barros ◽  
Caio de Oliveira ◽  
Newton Verbisck ◽  
...  
Keyword(s):  
Snake Venom ◽  
Bacterial Resistance ◽  
Specific Activity ◽  
Biological Activities ◽  
Public Health Problem ◽  
Bacterial Biofilm ◽  
Antibiofilm Activity ◽  
Amino Acid Residues ◽  
Alternative Approach ◽  
First Time

Introduction: Bacterial resistance is a worldwide public health problem, requiring new therapeutic options. An alternative approach to this problem is the use of animal toxins, such as phospholipases (PLA2) isolated from snake venom, which have important biological activities. Bothrops erythromelas is one of the snake species in the Northeast of Brazil that attracts great medical-scientific interest. Here we aimed to purify and characterize a PLA2 from B. erythromelas, searching for heterologous activities against bacterial biofilm. Methods: Venom extraction and quantification were followed by RP-HPLC in C18 column, MALDI-ToF mass spectrometry and sequencing by Edman degradation. All experiments were monitored by specific activity using 4-nitro-3 (octanoyloxy) benzoic acid (4N3OBA) substrate. In addition, hemolytic tests and anti-bacterial tests including action against Escherichia coli, Staphylococcus aureus and Acinetobacter baumannii, were carried out. Moreover, tests of antibiofilm action against A. baumannii were also performed. Results: PLA2, after one purification step, presented 31 N-terminal amino acid residues, and molecular weight of 13656.4 Da with enzymatic activity confirmed in 0.06 µM concentration. Antibacterial activity against S. aureus (IC50 = 30.2 µM) and antibiofilm activity against A. baumannii (IC50 = 1.1 µM) were observed. Conclusions: This is the first time that PLA2 purified from B. erythromelas venom has appeared as an alternative candidate in studies of new antibacterial medicines.

scholarly journals Genetic determinants of penicillin tolerance inVibrio cholerae

2018 ◽  
Author(s):  
Anna I. Weaver ◽  
Shannon G. Murphy ◽  
Benjamin Umans ◽  
Srikar Tallavajhala ◽  
Ikenna Onyekwere ◽  
...  
Keyword(s):  
Cell Wall ◽  
Lipid A ◽  
Cell Damage ◽  
Cell Envelope ◽  
Active Role ◽  
Beta Lactam ◽  
Drug Induced ◽  
Cell Wall Biogenesis ◽  
Rod System ◽  
Sphere Formation

AbstractMany bacteria are resistant to killing (“tolerant”) by typically bactericidal antibiotics due to their ability to counteract drug-induced cell damage.Vibrio cholerae, the cholera agent, displays an unusually high tolerance to diverse inhibitors of cell wall synthesis. Exposure to these agents, which in other bacteria leads to lysis and death, results in a breakdown of the cell wall and subsequent sphere formation inV. cholerae. Spheres readily recover to rod-shaped cells upon antibiotic removal, but the mechanisms mediating the recovery process are not well-characterized. Here, we found that the mechanisms of recovery are dependent on environmental conditions. Interestingly, on agarose pads, spheres undergo characteristic stages during the restoration of rod shape. Drug inhibition and microscopy experiments suggest that class A Penicillin Binding Proteins (aPBPs) play a more active role than the Rod system, especially early in sphere recovery. TnSeq analyses revealed that LPS and cell wall biogenesis genes as well as the sigma E cell envelope stress response were particularly critical for recovery. LPS core and O-antigen appear to be more critical for sphere formation/integrity and viability than Lipid A modifications. Overall, our findings demonstrate that the outer membrane is a key contributor to beta lactam tolerance and suggest a role for aPBPs in cell wall biogenesis in the absence of rod-shape cues. Factors required for post-antibiotic recovery could serve as targets for antibiotic adjuvants that enhance the efficacy of antibiotics that inhibit cell wall biogenesis.

Antibiofilm effect of Temporin-L on Pseudomonas fluorescens, in static and dynamic conditions.

2020 ◽  
Author(s):  
Arianna Cirillo ◽  
Angela Di Somma ◽  
Alessia Romano ◽  
Federica Recupido ◽  
Sergio Caserta ◽  
...  
Keyword(s):  
Confocal Microscopy ◽  
Pseudomonas Fluorescens ◽  
Bacterial Growth ◽  
Biofilm Formation ◽  
Bacterial Resistance ◽  
Antibiofilm Activity ◽  
Host Immune System ◽  
Dynamic Conditions ◽  
Biofilm Architecture ◽  
Static Conditions

<p>Introduction</p> <p>Biofilm consists of a complex self-produced matrix of polysaccharides, DNA and proteins that </p> <p>protects bacteria from the environment including the host immune system and constitutes the main</p> <p>cause of bacterial resistance against antibiotics. Research is then focused on finding alternative </p> <p>antimicrobial substances able to either hamper biofilm formation or to prevent bacterial growth. </p> <p>Recently, we showed that the antimicrobial peptide Temporin-L impairs E.coli growth by inhibiting </p> <p>cell division (Di Somma et al.; 2020; BBA). Here we investigate the effect of Temporin-L (TL) on </p> <p>biofilm formation in Pseudomonas fluorescens (P. fluorescens) both in static and dynamic conditions, </p> <p>showing that TL displays antibiofilm properties. </p> <p>Materials and methods</p> <p>Biofilm formation in static conditions was performed on coverslips and analyzed by the Crystal Violet </p> <p>assay. Biofilm morphology was assessed using imaging techniques. Investigation of biofilms in </p> <p>dynamic conditions was performed in a flow chamber using a microfluidic system and images were </p> <p>recorded by confocal microscopy.</p> <p>Results</p> <p>The P. fluorescens cells were either grown in the presence of TL or incubated with the antimicrobial </p> <p>peptide after biofilm formation both in static and dynamic conditions using different concentrations </p> <p>of the peptide. When TL was added during cell growth, the peptide affected biofilm formation at 25 </p> <p>µM. Confocal microscopy demonstrated that at this concentration P. fluorescens cells were still alive</p> <p>but a clear disruption of the biofilm architecture was observed. These results had to be ascribed to a </p> <p>specific antibiofilm effect of TL. At 100 µM TL antibiofilm activity biofilm thickness was nearly </p> <p>negligible. </p> <p>When P. fluorescens cells were treated with TL following biofilm formation, confocal images </p> <p>demonstrated that the peptide exerted a strong antibiofilm effect leading to cell detachment and </p> <p>disruption the biofilm architecture. </p> <p>Discussion and Conclusions </p> <p>Investigation of TL effect on P. fluorescens showed that when added during bacterial growth this </p> <p>peptide exerted antibiofilm activity at low concentration impairing biofilm formation both in static </p> <p>and dynamic conditions, leaving most of bacterial cells still alive. However, confocal microscopy </p> <p>measurements could not detect the long necklace-like structures observed in E.coli indicating a </p> <p>different mechanism of action of TL on P. fluorescens. Furthermore, when TL was added to a </p> <p>preformed P. fluorescens biofilm, the peptide showed a strong antibiofilm activity both in static and </p> <p>dynamic conditions, suggesting that TL might penetrate biofilm architecture with a still unknown </p> <p>mechanism leading to disruption of P. fluorescens biofilm.</p>

Size-dependent antimycobacterial activity of titanium oxide nanoparticles against Mycobacterium tuberculosis

2019 ◽  
Vol 7 (27) ◽  
pp. 4338-4346 ◽  
Author(s):  
Vaikundamoorthy Ramalingam ◽  
Subramaniam Sundaramahalingam ◽  
Rajendran Rajaram
Keyword(s):  
Cell Wall ◽  
Mycobacterium Tuberculosis ◽  
Titanium Oxide ◽  
Metabolic Activity ◽  
Biofilm Formation ◽  
Antimycobacterial Activity ◽  
Oxide Nanoparticles ◽  
Antibiofilm Activity ◽  
Titanium Oxide Nanoparticles ◽  
Size Dependent

The titanium oxide nanoparticles showed excellent antibiofilm activity against Mycobacterium tuberculosis by inhibiting the colony formation and damage the cell wall leads to immature biofilm formation as well as inhibition of metabolic activity.

scholarly journals Potential Risk of Spreading Resistance Genes within Extracellular-DNA-Dependent Biofilms of Streptococcus mutans in Response to Cell Envelope Stress Induced by Sub-MICs of Bacitracin

2020 ◽  
Vol 86 (16) ◽  
Author(s):  
Ryo Nagasawa ◽  
Tsutomu Sato ◽  
Nobuhiko Nomura ◽  
Tomoyo Nakamura ◽  
Hidenobu Senpuku
Keyword(s):  
Cell Wall ◽  
Gene Transfer ◽  
Horizontal Gene Transfer ◽  
Biofilm Formation ◽  
Cell Envelope ◽  
Resistant Bacteria ◽  
Drug Resistant ◽  
Content Type ◽  
Drug Resistant Bacteria ◽  
Envelope Stress

ABSTRACT Antibiotics are used to treat or prevent some types of bacterial infection. The inappropriate use of antibiotics unnecessarily promotes antibiotic resistance and increases resistant bacteria, and controlling these bacteria is difficult. While the emergence of drug-resistant bacteria is a serious problem, the behavior of drug-resistant bacteria is not fully understood. In this study, we investigated the behavior of Streptococcus mutans, a major etiological agent of dental caries that is resistant to bacitracin, which is a cell wall-targeting antibiotic, and focused on biofilm formation in the presence of bacitracin. S. mutans UA159 most strongly induced extracellular DNA (eDNA)-dependent biofilm formation in the presence of bacitracin at 1/8× MIC. The ΔmbrC and ΔmbrD mutant strains, which lack bacitracin resistance, also formed biofilms in the presence of bacitracin at 1/2× MIC. This difference between the wild type and the mutants was caused by the induction of atlA expression in the mid-log phase. We also revealed that certain rgp genes involved in the synthesis of rhamnose-glucose polysaccharide related to cell wall synthesis were downregulated by bacitracin. In addition, glucosyltransferase-I was also involved in eDNA-dependent biofilm formation. The biofilm led to increased transformation efficiencies and promoted horizontal gene transfer. Biofilms were also induced by ampicillin and vancomycin, antibiotics targeting cell wall synthesis, suggesting that cell envelope stress triggers biofilm formation. Therefore, the expression of the atlA and rgp genes is regulated by S. mutans, which forms eDNA-dependent biofilms, promoting horizontal gene transfer in response to cell envelope stress induced by sub-MICs of antibiotics. IMPORTANCE Antibiotics have been reported to induce biofilm formation in many bacteria at subinhibitory concentrations. Accordingly, it is conceivable that the MIC against drug-sensitive bacteria may promote biofilm formation of resistant bacteria. Since drug-resistant bacteria have spread, it is important to understand the behavior of resistant bacteria. Streptococcus mutans is bacitracin resistant, and the 1/8× MIC of bacitracin, which is a cell wall-targeted antibiotic, induced eDNA-dependent biofilm formation. The ΔmbrC and ΔmbrD strains, which are not resistant to bacitracin, also formed biofilms in the presence of bacitracin at 1/2× MIC, and biofilms of both the wild type and mutants promoted horizontal gene transfer. Another cell wall-targeted antibiotic, vancomycin, showed effects on biofilms and gene transfer similar to those of bacitracin. Thus, treatment with cell wall-targeted antibiotics may promote the spread of drug-resistant genes in biofilms. Therefore, the behavior of resistant bacteria in the presence of antibiotics at sub-MICs should be investigated when using antibiotics.

scholarly journals Deficiency of RgpG Causes Major Defects in Cell Division and Biofilm Formation, and Deficiency of LytR-CpsA-Psr Family Proteins Leads to Accumulation of Cell Wall Antigens in Culture Medium by Streptococcus mutans

2017 ◽  
Vol 83 (17) ◽  
Author(s):  
Arpan De ◽  
Sumei Liao ◽  
Jacob P. Bitoun ◽  
Randy Roth ◽  
Wandy L. Beatty ◽  
...  
Keyword(s):  
Growth Rate ◽  
Cell Wall ◽  
Cell Division ◽  
Streptococcus Mutans ◽  
Biofilm Formation ◽  
Cell Envelope ◽  
Biosynthesis Pathway ◽  
Wild Type ◽  
Triple Mutant ◽  
Content Type

ABSTRACTStreptococcus mutansis known to possess rhamnose-glucose polysaccharide (RGP), a major cell wall antigen.S. mutansstrains deficient inrgpG, encoding the first enzyme of the RGP biosynthesis pathway, were constructed by allelic exchange. ThergpGdeficiency had no effect on growth rate but caused major defects in cell division and altered cell morphology. Unlike the coccoid wild type, thergpGmutant existed primarily in chains of swollen, “squarish” dividing cells. Deficiency ofrgpGalso causes significant reduction in biofilm formation (P< 0.01). Double and triple mutants with deficiency inbrpAand/orpsr, genes coding for the LytR-CpsA-Psr family proteins BrpA and Psr, which were previously shown to play important roles in cell envelope biogenesis, were constructed using thergpGmutant. There were no major differences in growth rates between the wild-type strain and thergpG brpAandrgpG psrdouble mutants, but the growth rate of thergpG brpA psrtriple mutant was reduced drastically (P< 0.001). Under transmission electron microscopy, both double mutants resembled thergpGmutant, while the triple mutant existed as giant cells with multiple asymmetric septa. When analyzed by immunoblotting, thergpGmutant displayed major reductions in cell wall antigens compared to the wild type, while little or no signal was detected with the double and triple mutants and thebrpAandpsrsingle mutants. These results suggest that RgpG inS. mutansplays a critical role in cell division and biofilm formation and that BrpA and Psr may be responsible for attachment of cell wall antigens to the cell envelope.IMPORTANCEStreptococcus mutans, a major etiological agent of human dental caries, produces rhamnose-glucose polysaccharide (RGP) as the major cell wall antigen. This study provides direct evidence that deficiency of RgpG, the first enzyme of the RGP biosynthesis pathway, caused major defects in cell division and morphology and reduced biofilm formation byS. mutans, indicative of a significant role of RGP in cell division and biofilm formation inS. mutans. These results are novel not only inS. mutans, but also other streptococci that produce RGP. This study also shows that the LytR-CpsA-Psr family proteins BrpA and Psr inS. mutansare involved in attachment of RGP and probably other cell wall glycopolymers to the peptidoglycan. In addition, the results also suggest that BrpA and Psr may play a direct role in cell division and biofilm formation inS. mutans. This study reveals new potential targets to develop anticaries therapeutics.

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