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Special Issue "The 7th International Symposium on Antimicrobial Peptides (AMP2020): Recent Advances in Antimicrobial Peptides"

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Microbiology".

Deadline for manuscript submissions: closed (31 August 2020).

Special Issue Editors

Prof. Dr. Djamel Drider
Website
Guest Editor
Lille University, Unit of Research BIOECOAGRO INRA 1158, 59655 Villeneuve d’Ascq, France
Interests: cheese; PCR; molecular biology; genetics; microbiology; antimicrobials; food safety; food microbiology; antibacterial activity; probiotics; mycology; salmonella; lactic acid bacteria; bacteriocins; listeria monocytogenes; antimicrobial peptides; foodborne pathogens; listeria
Special Issues and Collections in MDPI journals
Dr. Javier Pizarro-Cerda
Website
Guest Editor
Institut Pasteur, Paris, France
Interests: antimicrobial peptides; bacteria-host interactions; systems biology of infection

Special Issue Information

Dear Colleagues,

The 7th International Symposium on Antimicrobial Peptides (AMP2020) will take place at the Institut Pasteur in Paris (France) from 3 to 5 June 2020 (http://www.AMP2020.conferences-pasteur.org). Research on antimicrobial peptides has traditionally been a fascinating field dedicated to understanding the multifaceted functions of these natural molecules produced in all living organisms.

The time has come to consider antimicrobial peptides as novel therapeutic options because of their potent antibiotic activity and often narrow target spectrum, which can be critical to tackle multidrug-resistant bacteria spreading worldwide and threating humans, animals, and our environment. Indeed, according to the O’Neil report (http://www.bsac.org.uk/securing-new-drugs-for-future-generations/), by 2050, more people will die in the world from infectious diseases than from any other illness. Actions are therefore needed now to avoid this potentially dramatic horizon.

AMP200 is a friendly conference gathering experts, industrialists, and young scientists interested in discussing, throughout the duration of this exciting symposium, the most recent advances on antimicrobial peptides, as well as their forthcoming applications.

The scientific committee of AMP2020 will dedicate a Special Issue of the International Journal of Molecular Sciences (https://www.mdpi.com/journal/ijms) to covering major topics and critical findings discussed during the symposium. IJMS is an open access resource with an impact factor of 4.18.

Details related to this Special Issue and conditions of publication are available online. For any further information, please feel free to contact the guest editors.

Prof. Dr. Djamel Drider
Dr. Javier Pizarro-Cerda
Guest Editors

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Published Papers (4 papers)

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Research

Open AccessArticle
Antimicrobial Peptides with Enhanced Salt Resistance and Antiendotoxin Properties
Int. J. Mol. Sci. 2020, 21(18), 6810; https://doi.org/10.3390/ijms21186810 - 16 Sep 2020
Abstract
A strategy was described to design antimicrobial peptides (AMPs) with enhanced salt resistance and antiendotoxin activities by linking two helical AMPs with the Ala-Gly-Pro (AGP) hinge. Among the designed peptides, KR12AGPWR6 demonstrated the best antimicrobial activities even in high salt conditions (NaCl ~300 [...] Read more.
A strategy was described to design antimicrobial peptides (AMPs) with enhanced salt resistance and antiendotoxin activities by linking two helical AMPs with the Ala-Gly-Pro (AGP) hinge. Among the designed peptides, KR12AGPWR6 demonstrated the best antimicrobial activities even in high salt conditions (NaCl ~300 mM) and possessed the strongest antiendotoxin activities. These activities may be related to hydrophobicity, membrane-permeability, and α-helical content of the peptide. Amino acids of the C-terminal helices were found to affect the peptide-induced permeabilization of LUVs, the α-helicity of the designed peptides under various LUVs, and the LPS aggregation and size alternation. A possible model was proposed to explain the mechanism of LPS neutralization by the designed peptides. These findings could provide a new approach for designing AMPs with enhanced salt resistance and antiendotoxin activities for potential therapeutic applications. Full article
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Open AccessArticle
Metabolic Shift of an Isogenic Strain of Enterococcus faecalis 14, Deficient in Its Own Bacteriocin Synthesis, as Revealed by a Transcriptomic Analysis
Int. J. Mol. Sci. 2020, 21(13), 4653; https://doi.org/10.3390/ijms21134653 - 30 Jun 2020
Abstract
The production of antimicrobial molecules often involves complex biological pathways. This study aimed at understanding the metabolic and physiological networks of enterocin EntDD14-associated function, in the bacteriocinogenic strain, Enterococcus faecalis 14. A global and comparative transcriptomic study was carried out on E. faecalis [...] Read more.
The production of antimicrobial molecules often involves complex biological pathways. This study aimed at understanding the metabolic and physiological networks of enterocin EntDD14-associated function, in the bacteriocinogenic strain, Enterococcus faecalis 14. A global and comparative transcriptomic study was carried out on E. faecalis 14 and its isogenic mutant Δbac, inactivated in genes coding for EntDD14. The in vitro ability to form biofilm on polystyrene plates was assessed by the crystal violet method, while the cytotoxicity on human colorectal adenocarcinoma Caco-2 cells was determined by the Cell Counting Kit-8. Transcriptomic data revealed that 71 genes were differentially expressed in both strains. As expected, genes coding for EntDD14 were downregulated in the Δbac mutant, whereas the other 69 genes were upregulated. Upregulated genes were associated with phage-related chromosomal islands, biofilm formation capability, resistance to environmental stresses, and metabolic reprogramming. Interestingly, the Δbac mutant showed an improved bacterial growth, a high capacity to form biofilm on inanimate surfaces and a very weak cytotoxicity level. These multiple metabolic rearrangements delineate a new line of defense to counterbalance the loss of EntDD14. Full article
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Open AccessArticle
Antimicrobial Peptides Display Strong Synergy with Vancomycin Against Vancomycin-Resistant E. faecium, S. aureus, and Wild-Type E. coli
Int. J. Mol. Sci. 2020, 21(13), 4578; https://doi.org/10.3390/ijms21134578 - 27 Jun 2020
Cited by 2
Abstract
There is an urgent and imminent need to develop new antimicrobials to fight against antibiotic-resistant bacterial and fungal strains. In this study, a checkerboard method was used to evaluate the synergistic effects of the antimicrobial peptide P-113 and its bulky non-nature amino acid [...] Read more.
There is an urgent and imminent need to develop new antimicrobials to fight against antibiotic-resistant bacterial and fungal strains. In this study, a checkerboard method was used to evaluate the synergistic effects of the antimicrobial peptide P-113 and its bulky non-nature amino acid substituted derivatives with vancomycin against vancomycin-resistant Enterococcus faecium, Staphylococcus aureus, and wild-type Escherichia coli. Boron-dipyrro-methene (BODIPY) labeled vancomycin was used to characterize the interactions between the peptides, vancomycin, and bacterial strains. Moreover, neutralization of antibiotic-induced releasing of lipopolysaccharide (LPS) from E. coli by the peptides was obtained. Among these peptides, Bip-P-113 demonstrated the best minimal inhibitory concentrations (MICs), antibiotics synergism, bacterial membrane permeabilization, and supernatant LPS neutralizing activities against the bacteria studied. These results could help in developing antimicrobial peptides that have synergistic activity with large size glycopeptides such as vancomycin in therapeutic applications. Full article
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Open AccessArticle
Two Distinct C-Type Lysozymes in Goldfish: Molecular Characterization, Antimicrobial Potential, and Transcriptional Regulation in Response to Opposing Effects of Bacteria/Lipopolysaccharide and Dexamethasone/Leptin
Int. J. Mol. Sci. 2020, 21(2), 501; https://doi.org/10.3390/ijms21020501 - 13 Jan 2020
Abstract
Lysozymes are key antimicrobial peptides in the host innate immune system that protect against pathogen infection. In this study, the full-length cDNAs of two c-type lysozymes (gfLyz-C1 and gfLyz-C2) were cloned from goldfish (Carassius auratus). The structural domains, three-dimensional structures, and [...] Read more.
Lysozymes are key antimicrobial peptides in the host innate immune system that protect against pathogen infection. In this study, the full-length cDNAs of two c-type lysozymes (gfLyz-C1 and gfLyz-C2) were cloned from goldfish (Carassius auratus). The structural domains, three-dimensional structures, and amino acid sequences of gfLyz-C1 and gfLyz-C2 were highly comparable, as the two proteins shared 89.7% sequence identity. The gfLyz-C1 and gfLyz-C2 recombinant proteins were generated in the insoluble fractions of an Escherichia coli system. Based on the results of lysoplate and turbidimetric assays, gfLyz-C1 and gfLyz-C2 showed broad-spectrum antimicrobial properties with high levels of activity against Micrococcus lysodeikticus, Vibrio parahemolyticus, and Edwardsiella tarda, and relatively low activity against E. coli. Both gfLyz-C1 and gfLyz-C2 mRNAs were mainly expressed in the trunk kidney and head kidney, and gfLyz-C1 was expressed at much higher levels than gfLyz-C2 in the corresponding tissues. The expression of the gfLyz-C1 and gfLyz-C2 transcripts in the trunk kidney and head kidney was induced in these tissues by challenge with heat-inactivated E. coli and lipopolysaccharides (LPS), and the transcriptional responses of gfLyz-C1 were more intense. In goldfish primary trunk kidney cells, the levels of the gfLyz-C1 and gfLyz-C2 transcripts were upregulated by heat-inactivated E. coli, V. parahemolyticus, and E. tarda, as well as LPS, and downregulated by treatment with dexamethasone and leptins. Overall, this study may provide new insights that will improve our understanding of the roles of c-type lysozymes in the innate immunity of cyprinid fish, including the structural and phylogenetic characteristics, antimicrobial effects, and regulatory mechanism. Full article
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