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Molecular Advances in Biotechnological Approaches to Developing Effective Antimicrobial Agents
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Molecular Advances in Biotechnological Approaches to Developing Effective Antimicrobial Agents

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

Deadline for manuscript submissions: closed (31 July 2024) | Viewed by 3440

Special Issue Editor

Dr. José M. Pérez De la Lastra

E-Mail Website
Guest Editor
Biotechnology of Macromolcules, Instituto de Productos Naturales y Agrobiología, CSIC, 28006 Madrid, Spain
Interests: biotechnology; macromolecules; antimicrobials; IgY antibodies; peptides; epitopes

Special Issue Information

Dear Colleagues,

Both antimicrobial peptides and IgY antibodies represent fascinating fields of study in biotechnology, offering promising avenues for the development of novel antimicrobial treatments and immunotherapies. Their potential to combat drug-resistant pathogens and provide effective alternatives to conventional antibiotics has sparked considerable interest in their application in various medical and agricultural settings.

In the context of antimicrobial applications, IgY antibodies have been explored as a potential defense against infectious agents. Researchers have successfully developed specific IgY antibodies targeting various pathogens, including bacteria and viruses for use in passive immunization strategies. These approaches offer an alternative to conventional antibiotics and can be particularly useful in scenarios where antibiotic resistance poses a significant challenge.

This Special Issue aims to provide recent insights and potential applications for developing innovative and effective antimicrobial strategies and on the challenges faced in translating these discoveries into clinically viable treatments. The topics covered range from the discovery and design of novel antimicrobial peptides to the engineering and optimization of IgY antibodies for combating infectious diseases.

Dr. José M. Pérez De la Lastra
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. 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.

Keywords

  • biotechnological
  • antimicrobial agents
  • IgY antibodies
  • peptides
  • drug resistance
  • antimicrobial resistance (AMR)
  • drug-resistant fungi
  • drug-resistant viruses

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Published Papers (3 papers)

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Research

28 pages, 1855 KiB  
Article
Antifungal Peptides with Unexpected Structure from a Library of Synthetic Analogs of Host-Defense Peptide Rigin
by Marina Porras, Dácil Hernández and Alicia Boto
Int. J. Mol. Sci. 2025, 26(5), 1900; https://doi.org/10.3390/ijms26051900 - 22 Feb 2025
Viewed by 542
Abstract
Rising antifungal resistance prompted the World Health Organization and the Food and Agriculture Organization to bring attention to the consequences of this threat to human, animal, and environmental health, and food security. In addition, there is an alarming cross-species pathogenicity. New antifungal agents [...] Read more.
Rising antifungal resistance prompted the World Health Organization and the Food and Agriculture Organization to bring attention to the consequences of this threat to human, animal, and environmental health, and food security. In addition, there is an alarming cross-species pathogenicity. New antifungal agents are urgently needed, preferably with a low induction of antimicrobial resistance (AMR). Among the most promising novel antimicrobials are the host-defense peptides, which present potent anti-infective properties and elicit low or negligible AMR. The rapid creation of libraries of host-defense peptides is highlighted by the synthesis of analogs of the immunomodulator and antimicrobial peptide rigin. Starting from smaller fragments incorporating hydroxyproline customizable units, which can be selectively cleaved and modified to give different lateral chains and N-substituents, two fragment libraries were built. Then the fragments were combined to give a library of rigin analogs, some of which displayed a potent antifungal activity not observed in the natural peptide. Surprisingly, the most active ones were N-substituted and lateral-chain protected analogs, while the free cationic peptides displayed low direct activity. This work shows that the strategy of combining site-selective peptide modification and a combinatorial approach can provide peptide-diverse libraries, where unexpected drug leads may be identified. Full article
(This article belongs to the Special Issue Molecular Advances in Biotechnological Approaches to Developing Effective Antimicrobial Agents)
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30 pages, 3746 KiB  
Article
Short Synthesis of Structurally Diverse N-Acylhomoserine Lactone Analogs and Discovery of Novel Quorum Quenchers Against Gram-Negative Pathogens
by Marina Porras, Dácil Hernández and Alicia Boto
Int. J. Mol. Sci. 2025, 26(4), 1775; https://doi.org/10.3390/ijms26041775 - 19 Feb 2025
Viewed by 483
Abstract
Quorum quenchers are emerging as an alternative to conventional antimicrobials, since they hinder the development of virulence or resistance mechanisms but without killing the microorganisms, thus, reducing the risk of antimicrobial resistance. Many quorum quenchers are analogs of the natural quorum-sensing signaling molecules [...] Read more.
Quorum quenchers are emerging as an alternative to conventional antimicrobials, since they hinder the development of virulence or resistance mechanisms but without killing the microorganisms, thus, reducing the risk of antimicrobial resistance. Many quorum quenchers are analogs of the natural quorum-sensing signaling molecules or autoinducers. Thus, different analogs of natural N-acylhomoserine lactones (AHLs) have been reported for controlling virulence or reducing the production of biofilms in Gram-negative pathogens. Herein we report the preparation of AHL analogs with a variety of N-substituents in just two steps from readily available N-substituted hydroxyproline esters. The substrates underwent an oxidative radical scission of the pyrrolidine ring. The resulting N-substituted β-aminoaldehyde underwent reduction and in situ cyclization to give a variety of homoserine lactones, with N- and N,N-substituted amino derivatives and with high optical purity. The libraries were screened for the inhibition of violacein production in Chromobacterium violaceum, a Gram-negative pathogen. For the first time, N,N-disubstituted AHL analogs were studied. Several N-sulfonyl derivatives, one carbamoyl, and one N-alkyl-N-sulfonyl homoserine lactone displayed a promising inhibitory activity. Moreover, they did not display microbicide action against S. aureus, C. jejuni, S. enterica, P. aeruginosa, and C. albicans, confirming a pure QQ activity. The determination of structure–activity relationships and in silico ADME studies are also reported, which are valuable for the design of next generations QQ agents. Full article
(This article belongs to the Special Issue Molecular Advances in Biotechnological Approaches to Developing Effective Antimicrobial Agents)
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11 pages, 4001 KiB  
Article
Preparation of Bispecific IgY-scFvs Inhibition Adherences of Enterotoxigenic Escherichia coli (K88 and F18) to Porcine IPEC-J2 Cell
by Luqing Yang, Yuanhe Yang, Anguo Liu, Siqi Lei and Pingli He
Int. J. Mol. Sci. 2024, 25(7), 3638; https://doi.org/10.3390/ijms25073638 - 25 Mar 2024
Cited by 2 | Viewed by 1766
Abstract
Enterotoxigenic Escherichia coli (ETEC) strains are significant contributors to postweaning diarrhea in piglets. Of the ETEC causing diarrhea, K88 and F18 accounted for 92.7%. Despite the prevalence of ETEC K88 and F18, there is currently no effective vaccine available due to the diversity [...] Read more.
Enterotoxigenic Escherichia coli (ETEC) strains are significant contributors to postweaning diarrhea in piglets. Of the ETEC causing diarrhea, K88 and F18 accounted for 92.7%. Despite the prevalence of ETEC K88 and F18, there is currently no effective vaccine available due to the diversity of these strains. This study presents an innovative approach by isolating chicken-derived single-chain variable fragment antibodies (scFvs) specific to K88 and F18 fimbrial antigens from chickens immunized against these ETEC virulence factors. These scFvs effectively inhibited adhesion of K88 and F18 to porcine intestinal epithelial cells (IPEC-J2), with the inhibitory effect demonstrating a dose-dependent increase. Furthermore, a bispecific scFv was designed and expressed in Pichia pastoris. This engineered construct displayed remarkable potency; at a concentration of 25.08 μg, it significantly reduced the adhesion rate of ETEC strains to IPEC-J2 cells by 72.10% and 69.11% when challenged with either K88 or F18 alone. Even in the presence of both antigens, the adhesion rate was notably decreased by 57.92%. By targeting and impeding the initial adhesion step of ETEC pathogenesis, this antibody-based intervention holds promise as a potential alternative to antibiotics, thereby mitigating the risks associated with antibiotic resistance and residual drug contamination in livestock production. Overall, this study lays the groundwork for the development of innovative treatments against ETEC infections in piglets. Full article
(This article belongs to the Special Issue Molecular Advances in Biotechnological Approaches to Developing Effective Antimicrobial Agents)
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