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Antibiotics
Special Issues
New Potent Antibacterial Agents
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New Potent Antibacterial Agents

A special issue of Antibiotics (ISSN 2079-6382). This special issue belongs to the section "Novel Antimicrobial Agents".

Deadline for manuscript submissions: closed (30 July 2021) | Viewed by 15183

Special Issue Editor

Prof. Dr. Muriel Masi

E-Mail Website
Guest Editor
1. MCT, INSERM U1261, UMR_MD1, Aix-Marseille University & IRBA SSA, 27 Boulevard Jean Moulin, 13005 Marseille, France
2. Synchrotron SOLEIL, L’Orme des Merisiers, Départementale 128, 91190 Saint-Aubin, France
Interests: bacterial envelope permeability; membrane transport; antibiotic resistance

Special Issue Information

Dear Colleagues,

Bacteria have developed several mechanisms to circumvent antibiotic activity, causing therapeutic failures. Faced with the worldwide problem of antibiotic resistance, there is an urgent need to discover and develop new antibacterial agents.

In this Special Issue, new potent antibacterial agents with mechanical and structural varieties will be considered as therapeutic approaches to defeat both Gram-positive and Gram-negative pathogens. We will cover the development of new antibiotics resulting from research on medicinal chemistry and synthetic biology, bioactive agents such as bacteriophages and bacteriocins, antibiotic interactions, and adjuvants that target the bacterial lifecycle (such as virulence and communication) or drug resistance mechanisms (such as antibiotic efflux and permeation). All types of articles falling within the scope of the above research areas are welcome.

Manuscript Submission Information

The general timeframe for a Special Issue is about 6 months. Authors can submit papers during this timeframe. 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. An initial decision based on peer-reviewed results could be provided by approximately 13 days after submission. The average publication time is approximately 32 days. Research articles, review articles, and short communications are invited.

Prof. Dr. Muriel Masi
Guest Editor

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

  • Antibiotics
  • Antibacterial agents
  • Antibiotic resistance
  • Drug discovery and screening
  • Mode of action
  • Drug transport

Published Papers (5 papers)

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Research

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8 pages, 1460 KiB  
Article
Antibacterial Activity of LCB10-0200 against Klebsiella pneumoniae
by Sang-Hun Oh, Young-Rok Kim, Hee-Soo Park, Kyu-Man Oh, Young-Lag Cho and Jin-Hwan Kwak
Antibiotics 2021, 10(10), 1185; https://doi.org/10.3390/antibiotics10101185 - 29 Sep 2021
Viewed by 1906
Abstract
Klebsiella pneumoniae is one of the important clinical organisms that causes various infectious diseases, including urinary tract infections, necrotizing pneumonia, and surgical wound infections. The increase in the incidence of multidrug-resistance K. pneumoniae is a major problem in public healthcare. Therefore, a novel [...] Read more.
Klebsiella pneumoniae is one of the important clinical organisms that causes various infectious diseases, including urinary tract infections, necrotizing pneumonia, and surgical wound infections. The increase in the incidence of multidrug-resistance K. pneumoniae is a major problem in public healthcare. Therefore, a novel antibacterial agent is needed to treat this pathogen. Here, we studied the in vitro and in vivo activities of a novel antibiotic LCB10-0200, a siderophore-conjugated cephalosporin, against clinical isolates of K. pneumoniae. In vitro susceptibility study found that LCB10-0200 showed potent antibacterial activity against K. pneumoniae, including the beta-lactamase producing strains. The in vivo efficacy of LCB10-0200 was examined in three different mouse infection models, including systemic, thigh, and urinary tract infections. LCB10-0200 showed more potent in vivo activity than ceftazidime in the three in vivo models against the drug-susceptible and drug-resistant K. pneumoniae strains. Taken together, these results show that LCB10-0200 is a potential antibacterial agent to treat infection caused by K. pneumoniae. Full article
(This article belongs to the Special Issue New Potent Antibacterial Agents)
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11 pages, 1493 KiB  
Article
Peroxynitrous Acid Generated In Situ from Acidified H2O2 and NaNO2. A Suitable Novel Antimicrobial Agent?
by Martina Balazinski, Ansgar Schmidt-Bleker, Jörn Winter and Thomas von Woedtke
Antibiotics 2021, 10(8), 1003; https://doi.org/10.3390/antibiotics10081003 - 19 Aug 2021
Cited by 5 | Viewed by 2171
Abstract
Peroxynitrite (ONOO−) and peroxynitrous acid (ONOOH) are known as short acting reactive species with nitrating and oxidative properties, which are associated with their antimicrobial effect. However, to the best of our knowledge, ONOOH/ONOO- are not yet used as antimicrobial actives [...] Read more.
Peroxynitrite (ONOO−) and peroxynitrous acid (ONOOH) are known as short acting reactive species with nitrating and oxidative properties, which are associated with their antimicrobial effect. However, to the best of our knowledge, ONOOH/ONOO- are not yet used as antimicrobial actives in practical applications. The aim is to elucidate if ONOOH generated in situ from acidified hydrogen peroxide (H2O2) and sodium nitrite (NaNO2) may serve as an antimicrobial active in disinfectants. Therefore, the dose-response relationship and mutagenicity are investigated. Antimicrobial efficacy was investigated by suspension tests and mutagenicity by the Ames test. Tests were conducted with E. coli. For investigating the dose-response relationship, pH values and concentrations of H2O2 and NaNO2 were varied. The antimicrobial efficacy is correlated to the dose of ONOOH, which is determined by numerical computations. The relationship can be described by the efficacy parameter W, corresponding to the amount of educts consumed during exposure time. Sufficient inactivation was observed whenever W ≥ 1 mM, yielding a criterion for inactivation of E. coli by acidified H2O2 and NaNO2. No mutagenicity of ONOOH was noticed. While further investigations are necessary, results indicate that safe and effective usage of ONOOH generated from acidified H2O2 and NaNO2 as a novel active in disinfectants is conceivable. Full article
(This article belongs to the Special Issue New Potent Antibacterial Agents)
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17 pages, 2358 KiB  
Article
The Use of an Organo-Selenium Peptide to Develop New Antimicrobials That Target a Specific Bacteria
by Phat Tran, Jonathan Kopel, Joe A. Fralick and Ted W. Reid
Antibiotics 2021, 10(6), 611; https://doi.org/10.3390/antibiotics10060611 - 21 May 2021
Cited by 7 | Viewed by 2126
Abstract
This study examines the use of a covalently selenium-bonded peptide and phage that binds to the Yersinia pestis F1 antigen for the targeting and killing of E. coli expressing this surface antigen. Using a Ph.D.-12 phage-display library for affinity selection of the phage [...] Read more.
This study examines the use of a covalently selenium-bonded peptide and phage that binds to the Yersinia pestis F1 antigen for the targeting and killing of E. coli expressing this surface antigen. Using a Ph.D.-12 phage-display library for affinity selection of the phage which would bind the F1 antigen of Y. pestis, a phage displaying a peptide that binds the F1 antigen with high affinity and specificity was identified. Selenium was then covalently attached to the display phage and the corresponding F1-antigen-binding peptide. Both the phage and peptides with selenium covalently attached retained their binding specificity for the Y. pestis F1 antigen. The phage or peptide not labeled with selenium did not kill the targeted bacteria, while the phage or peptide labeled with selenium did. In addition, the seleno-peptide, expressing the F1 targeting sequence only, killed cells expressing the F1 antigen but not the parent strain that did not express the F1 antigen. Specifically, the seleno-peptide could kill eight logs of bacteria in less than two hours at a 10-µM concentration. These results demonstrate a novel approach for the development of an antibacterial agent that can target a specific bacterial pathogen for destruction through the use of covalently attached selenium and will not affect other bacteria. Full article
(This article belongs to the Special Issue New Potent Antibacterial Agents)
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18 pages, 4410 KiB  
Article
Discovery of Pyrrolidine-2,3-diones as Novel Inhibitors of P. aeruginosa PBP3
by Arancha López-Pérez, Stefan Freischem, Immanuel Grimm, Oliver Weiergräber, Andrew J. Dingley, María Pascual López-Alberca, Herbert Waldmann, Waldemar Vollmer, Kamal Kumar and Cuong Vuong
Antibiotics 2021, 10(5), 529; https://doi.org/10.3390/antibiotics10050529 - 04 May 2021
Cited by 11 | Viewed by 3872
Abstract
The alarming threat of the spread of multidrug resistant bacteria currently leaves clinicians with very limited options to combat infections, especially those from Gram-negative bacteria. Hence, innovative strategies to deliver the next generation of antibacterials are urgently needed. Penicillin binding proteins (PBPs) are [...] Read more.
The alarming threat of the spread of multidrug resistant bacteria currently leaves clinicians with very limited options to combat infections, especially those from Gram-negative bacteria. Hence, innovative strategies to deliver the next generation of antibacterials are urgently needed. Penicillin binding proteins (PBPs) are proven targets inhibited by β-lactam antibiotics. To discover novel, non-β-lactam inhibitors against PBP3 of Pseudomonas aeruginosa, we optimised a fluorescence assay based on a well-known thioester artificial substrate and performed a target screening using a focused protease-targeted library of 2455 compounds, which led to the identification of pyrrolidine-2,3-dione as a potential scaffold to inhibit the PBP3 target. Further chemical optimisation using a one-pot three-component reaction protocol delivered compounds with excellent target inhibition, initial antibacterial activities against P. aeruginosa and no apparent cytotoxicity. Our investigation revealed the key structural features; for instance, 3-hydroxyl group (R2) and a heteroaryl group (R1) appended to the N-pyrroldine-2,3-dione via methylene linker required for target inhibition. Overall, the discovery of the pyrrolidine-2,3-dione class of inhibitors of PBP3 brings opportunities to target multidrug-resistant bacterial strains and calls for further optimisation to improve antibacterial activity against P. aeruginosa. Full article
(This article belongs to the Special Issue New Potent Antibacterial Agents)
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Review

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23 pages, 8194 KiB  
Review
The Biology of Colicin M and Its Orthologs
by Dimitri Chérier, Delphine Patin, Didier Blanot, Thierry Touzé and Hélène Barreteau
Antibiotics 2021, 10(9), 1109; https://doi.org/10.3390/antibiotics10091109 - 14 Sep 2021
Cited by 8 | Viewed by 4027
Abstract
The misuse of antibiotics during the last decades led to the emergence of multidrug resistant pathogenic bacteria. This phenomenon constitutes a major public health issue. Consequently, the discovery of new antibacterials in the short term is crucial. Colicins, due to their antibacterial properties, [...] Read more.
The misuse of antibiotics during the last decades led to the emergence of multidrug resistant pathogenic bacteria. This phenomenon constitutes a major public health issue. Consequently, the discovery of new antibacterials in the short term is crucial. Colicins, due to their antibacterial properties, thus constitute good candidates. These toxin proteins, produced by E. coli to kill enteric relative competitors, exhibit cytotoxicity through ionophoric activity or essential macromolecule degradation. Among the 25 colicin types known to date, colicin M (ColM) is the only one colicin interfering with peptidoglycan biosynthesis. Accordingly, ColM develops its lethal activity in E. coli periplasm by hydrolyzing the last peptidoglycan precursor, lipid II, into two dead-end products, thereby leading to cell lysis. Since the discovery of its unusual mode of action, several ColM orthologs have also been identified based on sequence alignments; all of the characterized ColM-like proteins display the same enzymatic activity of lipid II degradation and narrow antibacterial spectra. This publication aims at being an exhaustive review of the current knowledge on this new family of antibacterial enzymes as well as on their potential use as food preservatives or therapeutic agents. Full article
(This article belongs to the Special Issue New Potent Antibacterial Agents)
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