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99 results for “Antimicrobial peptides”
Survival of antimicrobial peptide resistant Staphylococcus aureus in mealworm beetles (Tenebrio molitor) with manipulated AMPexpression
<p><span>Antimicrobial peptides (AMP) are essential immune effectors of multicellular organisms. Bacteria can evolve resistance to AMPs. Surprisingly, when used to challenge the insect <em>Tenebrio molitor</em>, <em>Staphylococcus aureus</em> resistant to an abundant beetle AMP (tenecin 1) and also pleiotropically to phagocytosis did not increase host mortality or bacterial load compared to infections with wild-type <em>S. aureus</em>. A possible explanation is that antimicrobial resistance is costly due to collaterally increased sensitivity of AMP-resistant strains to other immune effectors. Here, we studied the sensitivity of a group of AMP-resistant <em>S. aureus</em> strains (which are either resistant to tenecin 1 or a combination of both tenecin 1 and tenecin 2) to other immune effectors such as phenoloxidase (PO) and other AMPs (specifically tenecin 1, tenecin 2 and tenecin 4) <em>in vivo</em>. Using RNAi-based knockdown (KD), we investigated <em>S. aureus in vivo</em> survival in insect hosts lacking particular immune effectors. We found that all except one AMP-resistant strain displayed collateral sensitivity toward phenoloxidase. Moreover, some AMP-resistant mutant strains showed sensitivity to one or more components of the beetle AMP defence cocktail. Our findings are consistent with the idea that resistance to AMPs and phagocytosis does not translate into changes in virulence because it is balanced by collaterally increased sensitivity to other host immune effectors. AMP resistance fails to provide a net survival advantage to <em>S. aureus</em> in a host environment that is dominated by AMPs because of the greater sensitivity to other immune effectors.</span></p>
Data from: A synthetic cationic antimicrobial peptide inhibits inflammatory response and the NLRP3 inflammasome by neutralizing LPS and ATP
Antimicrobial peptides (AMPs) are one of the most important defense mechanisms against bacterial infections in insects, plants, non-mammalian vertebrates, and mammals. In the present study, a class of synthetic AMPs was evaluated for anti-inflammatory activity. One cationic AMP, GW-A2, demonstrated the ability to inhibit the expression levels of nitric oxide (NO), inducible NO synthase (iNOS), cyclooxygenase-2 (COX-2), tumor necrosis factor-α (TNF-α) and interleukin-6 (IL-6) in lipopolysaccharide (LPS)-activated macrophages. GW-A2 reduced LPS-induced increases in the phosphorylation of mitogen-activated protein kinase and protein kinase C-α/δ and the activation of NF-κB. GW-A2 also inhibited NLRP3 inflammasome activation induced by LPS and ATP. Furthermore, in the mice injected with LPS, GW-A2 reduced (1) the concentration of IL-1β, IL-6 and TNF-α in the serum; (2) the concentration of TNF-α in the peritoneal lavage; (3) the expression levels of iNOS, COX-2 and NLRP3 in the liver and lung; (4) the infiltration of polymorphonuclear neutrophils in the liver and lung. The underlying mechanisms for the anti-inflammatory activity of GW-A2 were found to be partially due to LPS and ATP neutralization. These results provide insights into how GW-A2 inhibits inflammation and the NLRP3 inflammasome and provide a foundation for the design of rational therapeutics for inflammation-related diseases.
Data from: Evidence for adaptation from standing genetic variation on an antimicrobial peptide gene in the mussel Mytilus edulis
Genome scans of population differentiation identify candidate loci for adaptation but provide little information on how selection has influenced the genetic structure of these loci. Following a genome scan, we investigated the nature of the selection responsible for the outlying differentiation observed between populations of the marine mussel Mytilus edulis at a leucine/arginine polymorphism (L31R) in the antimicrobial peptide MGD2. We analysed DNA sequence polymorphisms, allele frequencies and population differentiation of polymorphisms closely linked to L31R, and pairwise and third-order linkage disequilibria. An outlying level of population differentiation was observed at L31R only, while no departure from panmixia was observed at linked loci surrounding L31R, as in most of the genome. Selection therefore seems to affect L31R directly. Three hypotheses can explain the lack of differentiation in the chromosomal region close to L31R: (i) hitchhiking has occurred but migration and recombination subsequently erased the signal, (ii) selection was weak enough and recombination strong enough to limit the hitchhiking effect to a very small chromosomal region or (iii) selection acted on a pre-existing polymorphism (i.e. standing variation) at linkage equilibrium with its background. Linkage equilibrium was observed between L31R and linked polymorphisms in every population analysed, as expected under the three hypotheses. However, linkage disequilibrium was observed in some populations between pairs of loci located upstream and downstream to L31R, generating a complex pattern of third-order linkage disequilibria which is best explained by the hypothesis of selection on a pre-existing polymorphism. We hypothesise that selection could be either balanced, maintaining alleles at different frequencies depending on the pathogen community encountered locally by mussels, or intermittent, resulting in sporadic fluctuations in allele frequency.
Supplementary material 1 from: Al Tall Y, Al-Nassar B, Abualhaijaa A, Sabi SH, Almaaytah A (2023) The design and functional characterization of a novel hybrid antimicrobial peptide from Esculentin-1a and melittin. Pharmacia 70(1): 161-170. https://doi.org/10.3897/pharmacia.70.e97116
RP-HPLC analysis Chromatogram of BKR1 peptide
Candidate antimicrobial peptide sequences mined from the UniProtKB/Swiss-Prot database using AMPlify
<p>Here we provide the datasets used in the study of AMP mining from the UniProtKB/Swiss-Prot database (2022_02 release), as well as the predicted AMP sequences by AMPlify v2.0.0. </p>
The Assessment of Antimicrobial Peptides Against Fungal Infection
ClinicalTrials.gov study NCT05368948. IPD Sharing: Not stated. Countries: 0. Publications: 8.
Data from: A synthetic cationic antimicrobial peptide inhibits inflammatory response and the NLRP3 inflammasome by neutralizing LPS and ATP
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Survival of antimicrobial peptide resistant Staphylococcus aureus in mealworm beetles (Tenebrio molitor) with manipulated AMPexpression
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Data from: Evidence for adaptation from standing genetic variation on an antimicrobial peptide gene in the mussel Mytilus edulis
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Data from: Increased survival of experimentally evolved antimicrobial peptide-resistant Staphylococcus aureus in an animal host
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Data from: The potential for adaptive maintenance of diversity in antimicrobial peptides
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Data from: Transcriptome resources for the frogs Lithobates clamitans and Pseudacris regilla, emphasizing antimicrobial peptides and conserved loci for phylogenetics
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The role of NLRP3 in regulation of antimicrobial peptides and estrogen signaling in UPEC-infected bladder epithelial cells
GEO Series GSE243098. Homo sapiens. 12 samples. Type: Expression profiling by array.
RNA-seq of Bacillus subtilis WT W168 treated with the antimicrobial peptide YydF (0.5µM) compared to untreated control
GEO Series GSE140605. Bacillus subtilis subsp. subtilis str. 168. 6 samples. Type: Expression profiling by high throughput sequencing.
Gene expression analysis of HL-60 cells treated with antimicrobial peptide ChMAP-28
GEO Series GSE118397. Homo sapiens. 3 samples. Type: Expression profiling by array.
A dual-mechanism antimicrobial peptide with antimutagenic activity targets the replisome and induces cell envelope stress
GEO Series GSE276254. Escherichia coli. 51 samples. Type: Expression profiling by high throughput sequencing.
Generic and specific adaptative response of S. pneumoniae to challenge with three distinct antimicrobial peptides
GEO Series GSE16491. Streptococcus pneumoniae D39; Streptococcus pneumoniae. 6 samples. Type: Expression profiling by array.
Human cathelicidin antimicrobial peptide LL37 effect on human neonatal epidermal keratinocytes (NHEKs).
GEO Series GSE49472. Homo sapiens. 12 samples. Type: Expression profiling by array.
Peptide YY: a Paneth cell antimicrobial peptide that maintains Candida gut commensalism.
GEO Series GSE229566. Candida albicans. 12 samples. Type: Expression profiling by high throughput sequencing.
Responses of S. aureus to stress caused by sublethal concentration of cationic antimicrobial peptides
GEO Series GSE15800. Staphylococcus aureus. 12 samples. Type: Expression profiling by array.
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