Bioinformatic Analysis of Genome-Predicted Bat Cathelicidins

Lastra, José Manuel Pérez de la; Asensio-Calavia, Patricia; González-Acosta, Sergio; Baca-González, Victoria; Morales-delaNuez, A.

doi:10.3390/molecules26061811

Cited by 12 publications

(15 citation statements)

References 45 publications

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“…The large diversity of cationic peptides has been hypothesized to derive from their antibacterial role in combating the distinct pathogenic microorganism issues faced by each host organism (119). Nature contains an almost unlimited number of peptide drugs that need to be pharmacologically characterized (121,122). Templates for the development of new antimicrobial agents can be found from creatures that live in germ-filled habitats, which can penetrate bacterial membranes (123, 124).…”

Section: Antimicrobial Peptidesmentioning

confidence: 99%

Antimicrobial Resistance in the COVID-19 Landscape: Is There an Opportunity for Anti-Infective Antibodies and Antimicrobial Peptides?

et al. 2022

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Although COVID-19 has captured most of the public health attention, antimicrobial resistance (AMR) has not disappeared. To prevent the escape of resistant microorganisms in animals or environmental reservoirs a “one health approach” is desirable. In this context of COVID-19, AMR has probably been affected by the inappropriate or over-use of antibiotics. The increased use of antimicrobials and biocides for disinfection may have enhanced the prevalence of AMR. Antibiotics have been used empirically in patients with COVID-19 to avoid or prevent bacterial coinfection or superinfections. On the other hand, the measures to prevent the transmission of COVID-19 could have reduced the risk of the emergence of multidrug-resistant microorganisms. Since we do not currently have a sterilizing vaccine against SARS-CoV-2, the virus may still multiply in the organism and new mutations may occur. As a consequence, there is a risk of the appearance of new variants. Nature-derived anti-infective agents, such as antibodies and antimicrobial peptides (AMPs), are very promising in the fight against infectious diseases, because they are less likely to develop resistance, even though further investigation is still required.

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Section: Antimicrobial Peptidesmentioning

confidence: 99%

Antimicrobial Resistance in the COVID-19 Landscape: Is There an Opportunity for Anti-Infective Antibodies and Antimicrobial Peptides?

et al. 2022

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“…When the Talpa occidentalis cathelicidin precursor was analyzed, it was shown to have the same cleavage site as most cathelicidins [ 36 ]. Hence, the site for elastase cutting site of the putative peptide was predicted for the first valine or alanine of the amino acid sequence from the fourth exon.…”

Section: Resultsmentioning

confidence: 99%

“…The presence of a conserved cathelin-like domain was used to determine the nature of the cathelicidin family. The bioinformatic analysis of cathelicidins seems to be effective in finding the biologically active region of the protein, allowing the sequence of the active peptide to be obtained, as well as the prediction of the peptides most likely to be active [ 36 ]. In our analysis, the common shrew ( Sorex araneus ) was the only Eulipotyphla cathelicidin from which no biological activity was predicted, being the one with the smallest a-helix region, with no positive net charge, less hydrophobicity, and a distinct mode of interaction with simulated membranes.…”

Section: Discussionmentioning

confidence: 99%

Antimicrobial Activity of Cathelicidin-Derived Peptide from the Iberian Mole Talpa occidentalis

Otazo-Pérez

Asensio-Calavia²,

González-Acosta³

et al. 2022

Vaccines

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The immune systems of all vertebrates contain cathelicidins, a family of antimicrobial peptides. Cathelicidins are a type of innate immune effector that have a number of biological functions, including a well-known direct antibacterial action and immunomodulatory function. In search of new templates for antimicrobial peptide discovery, we have identified and characterized the cathelicidin of the small mammal Talpa occidentalis. We describe the heterogeneity of cathelicidin in the order Eulipotyphla in relation to the Iberian mole and predict its antibacterial activity using bioinformatics tools. In an effort to correlate these findings, we derived the putative active peptide and performed in vitro hemolysis and antimicrobial activity assays, confirming that Iberian mole cathelicidins are antimicrobial. Our results showed that the Iberian mole putative peptide, named To-KL37 (KLFGKVGNLLQKGWQKIKNIGRRIKDFFRNIRPMQEA) has antibacterial and antifungal activity. Understanding the antimicrobial defense of insectivores may help scientists prevent the spread of pathogens to humans. We hope that this study can also provide new, effective antibacterial peptides for future drug development.

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“…The bacteria have a total of 14 strains, and their genomic/proteomic data were retrieved from the genome database of the National Center For Biotechnology Information (NCBI) database [41]. All the respective proteomes and genomes were retrieved in FASTA format [42].…”

Section: P Rettgeri Complete Proteome Retrievalmentioning

confidence: 99%

Designing a Recombinant Vaccine against Providencia rettgeri Using Immunoinformatics Approach

et al. 2022

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Antibiotic resistance (AR) is the resistance mechanism pattern in bacteria that evolves over some time, thus protecting the bacteria against antibiotics. AR is due to bacterial evolution to make itself fit to changing environmental conditions in a quest for survival of the fittest. AR has emerged due to the misuse and overuse of antimicrobial drugs, and few antibiotics are now left to deal with these superbug infections. To combat AR, vaccination is an effective method, used either therapeutically or prophylactically. In the current study, an in silico approach was applied for the design of multi-epitope-based vaccines against Providencia rettgeri, a major cause of traveler’s diarrhea. A total of six proteins: fimbrial protein, flagellar hook protein (FlgE), flagellar basal body L-ring protein (FlgH), flagellar hook-basal body complex protein (FliE), flagellar basal body P-ring formation protein (FlgA), and Gram-negative pili assembly chaperone domain proteins, were considered as vaccine targets and were utilized for B- and T-cell epitope prediction. The predicted epitopes were assessed for allergenicity, antigenicity, virulence, toxicity, and solubility. Moreover, filtered epitopes were utilized in multi-epitope vaccine construction. The predicted epitopes were joined with each other through specific GPGPG linkers and were joined with cholera toxin B subunit adjuvant via another EAAAK linker in order to enhance the efficacy of the designed vaccine. Docking studies of the designed vaccine construct were performed with MHC-I (PDB ID: 1I1Y), MHC-II (1KG0), and TLR-4 (4G8A). Findings of the docking study were validated through molecular dynamic simulations, which confirmed that the designed vaccine showed strong interactions with the immune receptors, and that the epitopes were exposed to the host immune system for proper recognition and processing. Additionally, binding free energies were estimated, which highlighted both electrostatic energy and van der Waals forces to make the complexes stable. Briefly, findings of the current study are promising and may help experimental vaccinologists to formulate a novel multi-epitope vaccine against P. rettgeri.

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Bioinformatic Analysis of Genome-Predicted Bat Cathelicidins

Cited by 12 publications

References 45 publications

Antimicrobial Resistance in the COVID-19 Landscape: Is There an Opportunity for Anti-Infective Antibodies and Antimicrobial Peptides?

Antimicrobial Resistance in the COVID-19 Landscape: Is There an Opportunity for Anti-Infective Antibodies and Antimicrobial Peptides?

Antimicrobial Activity of Cathelicidin-Derived Peptide from the Iberian Mole Talpa occidentalis

Designing a Recombinant Vaccine against Providencia rettgeri Using Immunoinformatics Approach

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