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Antibiotics
Special Issues
Antibiotics Acting on Cell Wall
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Antibiotics Acting on Cell Wall

A special issue of Antibiotics (ISSN 2079-6382).

Deadline for manuscript submissions: closed (30 April 2020) | Viewed by 13703

Special Issue Editors

Prof. Dr. Flavia Marinelli

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Guest Editor
Dipartimento di Biotecnologie e Scienze della Vita, Università degli Studi dell'Insubria, Via J.H. Dunant 3, 21100 Varese, Italy
Interests: actinomycetes; natural products; antibiotics; resistome; glycopeptides; lantibiotics
Special Issues, Collections and Topics in MDPI journals
Dr. Bohdan Ostash

E-Mail Website
Guest Editor
Department of Genetics and Biotechnology, Ivan Franko National University of Lviv, Hrushevskoho st 4, Rm 102, 79005 Lviv, Ukraine
Interests: actinobacterial genetics; genetic control of antibiotic production; strain improvement; genomics of secondary metabolism
Special Issues, Collections and Topics in MDPI journals
Dr. Olga Genilloud

E-Mail Website
Guest Editor
Fundación MEDINA, Centro de Excelencia en Investigación de Medicamentos Innovadores en Andalucía, Parque Tecnológico Ciencias de la Salud, Avenida del Conocimiento 34, Granada, Spain
Interests: natural products; drug discovery; antibiotics; antimicrobial resistance; natural product biosynthesis
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Cell walls are essential for bacterial and fungal shape and integrity. Consequently, peptidoglycan biosynthesis in bacteria is an optimal target for antibacterial agents. Many clinically successful antibiotics such as β-lactams and glycopeptides target bacterial cell wall assembly. Novel cell wall inhibitors have been discovered, and some of them (for instance, lantibiotics) are in preclinical studies. The fungal cell wall represents an essential target for antifungal therapies, and important antifungal drugs such as the derivatives of echinocandins are currently in clinical use for treating severe systemic infections. Emerging resistance to such antibacterial and antifungal agents is often mediated by modifications of cell wall biosynthesis and assembly. In some cases, the molecular mechanisms rendering cell walls resistant to antibiotic action still need to be fully understood.

This Special Issue aims to update the current knowledge of all aspects of chemical diversity, biology, and clinical use of cell wall inhibitors. Thus, we would like to invite the submissions of high-quality manuscripts and review articles addressing the mode of action of and the mechanisms of resistance to established drugs, novel antibiotics targeting bacterial and fungal cell walls, their biosynthetic studies, and clinical or potential impact. We also welcome the contributions covering the chemical diversity of and medical prospects for cell wall-active antibiotics (from natural or non-natural sources) as well as papers investigating the putative natural reservoirs of novel molecules and resistance genes.

Prof. Dr. Flavia Marinelli
Dr. Bohdan Ostash
Dr. Olga Genilloud
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 submissions that pass pre-check are 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. Antibiotics is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2900 CHF (Swiss Francs). 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.

Keywords

  • cell wall inhibitors
  • antibiotic resistance
  • antibiotic resistome
  • peptidoglycan
  • fungal cell wall
  • β-lactams
  • glycopeptides
  • lantibiotics
  • echinocandins
  • natural product research

Published Papers (3 papers)

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Research

11 pages, 1710 KiB  
Article
Squalamine and Aminosterol Mimics Inhibit the Peptidoglycan Glycosyltransferase Activity of PBP1b
by Adrien Boes, Jean Michel Brunel, Adeline Derouaux, Frédéric Kerff, Ahmed Bouhss, Thierry Touze, Eefjan Breukink and Mohammed Terrak
Antibiotics 2020, 9(7), 373; https://doi.org/10.3390/antibiotics9070373 - 02 Jul 2020
Cited by 9 | Viewed by 2911
Abstract
Peptidoglycan (PG) is an essential polymer of the bacterial cell wall and a major antibacterial target. Its synthesis requires glycosyltransferase (GTase) and transpeptidase enzymes that, respectively, catalyze glycan chain elongation and their cross-linking to form the protective sacculus of the bacterial cell. The [...] Read more.
Peptidoglycan (PG) is an essential polymer of the bacterial cell wall and a major antibacterial target. Its synthesis requires glycosyltransferase (GTase) and transpeptidase enzymes that, respectively, catalyze glycan chain elongation and their cross-linking to form the protective sacculus of the bacterial cell. The GTase domain of bifunctional penicillin-binding proteins (PBPs) of class A, such as Escherichia coli PBP1b, belong to the GTase 51 family. These enzymes play an essential role in PG synthesis, and their specific inhibition by moenomycin was shown to lead to bacterial cell death. In this work, we report that the aminosterol squalamine and mimic compounds present an unexpected mode of action consisting in the inhibition of the GTase activity of the model enzyme PBP1b. In addition, selected compounds were able to specifically displace the lipid II from the active site in a fluorescence anisotropy assay, suggesting that they act as competitive inhibitors. Full article
(This article belongs to the Special Issue Antibiotics Acting on Cell Wall)
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17 pages, 2037 KiB  
Article
A Silkworm Infection Model for In Vivo Study of Glycopeptide Antibiotics
by Aurora Montali, Francesca Berini, Maurizio Francesco Brivio, Maristella Mastore, Alessio Saviane, Silvia Cappellozza, Flavia Marinelli and Gianluca Tettamanti
Antibiotics 2020, 9(6), 300; https://doi.org/10.3390/antibiotics9060300 - 04 Jun 2020
Cited by 14 | Viewed by 4362
Abstract
Glycopeptide antibiotics (GPAs) are drugs of last resort for treating infections by Gram-positive bacteria. They inhibit bacterial cell wall assembly by binding to the d-Ala-d-Ala terminus of peptidoglycan precursors, leading to cell lysis. Vancomycin and teicoplanin are first generation GPAs, [...] Read more.
Glycopeptide antibiotics (GPAs) are drugs of last resort for treating infections by Gram-positive bacteria. They inhibit bacterial cell wall assembly by binding to the d-Ala-d-Ala terminus of peptidoglycan precursors, leading to cell lysis. Vancomycin and teicoplanin are first generation GPAs, while dalbavancin is one of the few, recently approved, second generation GPAs. In this paper, we developed an in vivo insect model to compare, for the first time, the efficacy of these three GPAs in curing Staphylococcus aureus infection. Differently from previous reports, Bombyx mori larvae were reared at 37 °C, and the course of infection was monitored, following not only larval survival, but also bacterial load in the insect body, hemocyte activity, phenoloxidase activity, and antimicrobial peptide expression. We demonstrated that the injection of S. aureus into the hemolymph of B. mori larvae led to a marked reduction of their survival rate within 24–48 h. GPAs were not toxic to the larvae and cured S. aureus infection. Dalbavancin was more effective than first generation GPAs. Due to its great advantages (i.e., easy and safe handling, low rearing costs, low antibiotic amount needed for the tests, no restrictions imposed by ethical and regulatory issues), this silkworm infection model could be introduced in preclinical phases—prior to the use of mice—accelerating the discovery/development rate of novel GPAs. Full article
(This article belongs to the Special Issue Antibiotics Acting on Cell Wall)
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15 pages, 3555 KiB  
Article
Identification and Heterologous Expression of the Biosynthetic Gene Cluster Encoding the Lasso Peptide Humidimycin, a Caspofungin Activity Potentiator
by Marina Sánchez-Hidalgo, Jesús Martín and Olga Genilloud
Antibiotics 2020, 9(2), 67; https://doi.org/10.3390/antibiotics9020067 - 07 Feb 2020
Cited by 13 | Viewed by 5343
Abstract
Humidimycin (MDN-0010) is a ribosomally synthesized and post-translationally modified peptide (RiPP) belonging to class I lasso peptides, and is structurally related to siamycins, which have been shown to have strong antimicrobial activities against Gram-positive bacteria and to possess anti-HIV activity. Humidimycin was isolated [...] Read more.
Humidimycin (MDN-0010) is a ribosomally synthesized and post-translationally modified peptide (RiPP) belonging to class I lasso peptides, and is structurally related to siamycins, which have been shown to have strong antimicrobial activities against Gram-positive bacteria and to possess anti-HIV activity. Humidimycin was isolated from the strain Streptomyces humidus CA-100629, and was shown to synergize the activity of the fungal cell wall inhibitor caspofungin. In this work, the biosynthetic gene cluster of humidimycin was identified by genome mining of S. humidus CA-100629, cloned by Gibson assembly, and heterologously expressed. Full article
(This article belongs to the Special Issue Antibiotics Acting on Cell Wall)
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