Venom peptides cathelicidin and lycotoxin cause strong inhibition of Escherichia coli ATP synthase

Azim, Sofiya; McDowell, Derek; Cartagena, Alec; Rodriguez, Ricky; Laughlin, Thomas F.; Ahmad, Zulfiqar

doi:10.1016/j.ijbiomac.2016.02.061

Cited by 32 publications

(23 citation statements)

References 57 publications

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“…As for the other groups, reports indicate their antibacterial character [14]. What is very interesting is that the composition of F2 fraction is quite similar to F1, although there is no LAAOs but there are SVMPs and, more importantly, cathelicidin-like antimicrobial peptides, which have a wide spectrum of antibacterial activity and high efficiency [15,16]. Despite this, the F1 fraction did not show any antibacterial properties in our tests.…”

Section: Discussionmentioning

confidence: 49%

Antimicrobial Activity of Protein Fraction from Naja ashei Venom against Staphylococcus epidermidis

et al. 2020

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One of the key problems of modern infectious disease medicine is the growing number of drug-resistant and multi-drug-resistant bacterial strains. For this reason, many studies are devoted to the search for highly active antimicrobial substances that could be used in therapy against bacterial infections. As it turns out, snake venoms are a rich source of proteins that exert a strong antibacterial effect, and therefore they have become an interesting research material. We analyzed Naja ashei venom for such antibacterial properties, and we found that a specific composition of proteins can act to eliminate individual bacterial cells, as well as the entire biofilm of Staphylococcus epidermidis. In general, we used ion exchange chromatography (IEX) to obtain 10 protein fractions with different levels of complexity, which were then tested against certified and clinical strains of S. epidermidis. One of the fractions (F2) showed exceptional antimicrobial effects both alone and in combination with antibiotics. The protein composition of the obtained fractions was determined using mass spectrometry techniques, indicating a high proportion of phospholipases A2, three-finger toxins, and L-amino acids oxidases in F2 fraction, which are most likely responsible for the unique properties of this fraction. Moreover, we were able to identify a new group of low abundant proteins containing the Ig-like domain that have not been previously described in snake venoms.

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Section: Discussionmentioning

confidence: 49%

Antimicrobial Activity of Protein Fraction from Naja ashei Venom against Staphylococcus epidermidis

et al. 2020

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“…The variety and spatial positioning of functional groups of inhibitors is one of the main reasons behind complete or partial inhibition of enzymes in general and ATP synthase in particular [57]. In previous studies, numerous instances of variable maximal inhibition of ATP synthase have been observed where wild-type or mutant enzymes were partially or incompletely inhibited by phytochemicals, peptides, NBD-Cl, NaN 3 , AlCl 3 , or ScCl 3 [5, 49, 55, 58, 59]. …”

Section: Discussionmentioning

confidence: 99%

Understanding the link between antimicrobial properties of dietary olive phenolics and bacterial ATP synthase

Amini

Liu

Ahmad

2017

International Journal of Biological Macromolecules

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The naturally occurring olive phenolics tyrosol, hydroxytyrosol, dihydroxyphenylglycol (DHPG), and oleuropein are known to have antioxidant, antitumor, and antibacterial properties. In the current study, we examined whether the antimicrobial properties of tyrosol, hydroxytyrosol, DHPG, and oleuropein were linked to the inhibition of bacterial ATP synthase. Tyrosol, hydroxytyrosol, DHPG, and oleuropein inhibited Escherichia coli wild-type and mutant membrane-bound F1Fo ATP synthase to variable degrees. The growth properties of wild-type, null, and mutant strains in presence of above olive phenolics were also abrogated to variable degrees on limiting glucose and succinate. Tyrosol and oleuropein synergistically inhibited the wild-type enzyme. Comparative wild-type and mutant F1Fo ATP synthase inhibitory profiles suggested that αArg-283 is an important residue and olive phenolics bind at the polyphenol binding pocket of ATP synthase. Growth patterns of wild-type, null, and mutant strains in the presence of tyrosol, hydroxytyrosol, DHPG, and oleuropein also hint at the possibility of additional molecular targets. Our results demonstrated that ATP synthase can be used as a molecular target and the antimicrobial properties of olive phenolics in general and tyrosol in particular can be linked to the binding and inhibition of bacterial ATP synthase.

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“…If traced back, our application allows detection of differential peptide profiles, providing a robust tool to discriminate not only strain-specific peptides, but true intraspecies differences among a set of biological replicates or even microorganism-phenotype variations such as those occurring between biofilm and planktonic populations. In this regard, the negative effect of certain peptide families on bacteria through different mechanisms is well known [55,56]. In this regard, our pipeline will just provide a candidate peptide list, but experimental approaches such as MS/MS experiments will never detect peptides that are inhibiting own bacterial growth.…”

Section: Resultsmentioning

confidence: 99%

Improving Phylogeny Reconstruction at the Strain Level Using Peptidome Datasets

et al. 2016

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Typical bacterial strain differentiation methods are often challenged by high genetic similarity between strains. To address this problem, we introduce a novel in silico peptide fingerprinting method based on conventional wet-lab protocols that enables the identification of potential strain-specific peptides. These can be further investigated using in vitro approaches, laying a foundation for the development of biomarker detection and application-specific methods. This novel method aims at reducing large amounts of comparative peptide data to binary matrices while maintaining a high phylogenetic resolution. The underlying case study concerns the Bacillus cereus group, namely the differentiation of Bacillus thuringiensis, Bacillus anthracis and Bacillus cereus strains. Results show that trees based on cytoplasmic and extracellular peptidomes are only marginally in conflict with those based on whole proteomes, as inferred by the established Genome-BLAST Distance Phylogeny (GBDP) method. Hence, these results indicate that the two approaches can most likely be used complementarily even in other organismal groups. The obtained results confirm previous reports about the misclassification of many strains within the B. cereus group. Moreover, our method was able to separate the B. anthracis strains with high resolution, similarly to the GBDP results as benchmarked via Bayesian inference and both Maximum Likelihood and Maximum Parsimony. In addition to the presented phylogenomic applications, whole-peptide fingerprinting might also become a valuable complementary technique to digital DNA-DNA hybridization, notably for bacterial classification at the species and subspecies level in the future.

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Venom peptides cathelicidin and lycotoxin cause strong inhibition of Escherichia coli ATP synthase

Cited by 32 publications

References 57 publications

Antimicrobial Activity of Protein Fraction from Naja ashei Venom against Staphylococcus epidermidis

Antimicrobial Activity of Protein Fraction from Naja ashei Venom against Staphylococcus epidermidis

Understanding the link between antimicrobial properties of dietary olive phenolics and bacterial ATP synthase

Improving Phylogeny Reconstruction at the Strain Level Using Peptidome Datasets

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