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Antibiotics
Special Issues
Antimicrobial Peptides and Host-Pathogen Interaction
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Antimicrobial Peptides and Host-Pathogen Interaction

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

Deadline for manuscript submissions: closed (15 November 2021) | Viewed by 9446

Special Issue Editor

Dr. Rokeya Sultana Rekha

E-Mail Website
Guest Editor
Department of Laboratory Medicine, Karolinska University Hospital, Stockholm, Sweden
Interests: infection biology; how different pathogen alter host defense mechanisms to survive in the host; antibiotic resistance and its underlying mechanisms; respiratory tract infection such as tuberculosis & pneumonia; autophagy; antimicrobial peptides and host-pathogen interaction

Special Issue Information

Dear Colleagues,

Antimicrobial peptides (AMPs) are known as host’s own antibiotics with a broad spectrum of antimicrobial activity. These peptides are able to kill a diverse range of microorganisms including bacteria, viruses, and fungi. AMPs are evolutionarily conserved and present in almost all living organisms including humans, mammals, vertebrates, invertebrates, plants, and insects. AMPs are the most important element of the innate defense system. This Special Issue seeks manuscript submissions on all aspects of antibacterial peptides, especially on how host and pathogen interact in different pathophysiological conditions and the role AMPs in modulating these interactions. All submission types, such as original research manuscripts, short communications, and reviews, are appreciated.

Dr. Rokeya Sultana Rekha
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

  • Antimicrobial peptides
  • Peptide antibiotics
  • Host defense peptides
  • Mechanism of action
  • Antimicrobial resistance
  • Host-directed therapy

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Published Papers (3 papers)

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Research

12 pages, 2782 KiB  
Article
Mechanistic Fingerprinting Reveals Kinetic Signatures of Resistance to Daptomycin and Host Defense Peptides in Streptococcus mitis-oralis
by Michael R. Yeaman, Liana C. Chan, Nagendra N. Mishra and Arnold S. Bayer
Antibiotics 2021, 10(4), 404; https://doi.org/10.3390/antibiotics10040404 - 8 Apr 2021
Cited by 2 | Viewed by 2534
Abstract
Streptococcus mitis-oralis (S. mitis-oralis) infections are increasingly prevalent in specific populations, including neutropenic cancer and endocarditis patients. S. mitis-oralis strains have a propensity to evolve rapid, high-level and durable resistance to daptomycin (DAP-R) in vitro and in vivo, although the mechanism(s) involved remain [...] Read more.
Streptococcus mitis-oralis (S. mitis-oralis) infections are increasingly prevalent in specific populations, including neutropenic cancer and endocarditis patients. S. mitis-oralis strains have a propensity to evolve rapid, high-level and durable resistance to daptomycin (DAP-R) in vitro and in vivo, although the mechanism(s) involved remain incompletely defined. We examined mechanisms of DAP-R versus cross-resistance to cationic host defense peptides (HDPs), using an isogenic S. mitis-oralis strain-pair: (i) DAP-susceptible (DAP-S) parental 351-WT (DAP MIC = 0.5 µg/mL), and its (ii) DAP-R variant 351-D10 (DAP MIC > 256 µg/mL). DAP binding was quantified by flow cytometry, in-parallel with temporal (1–4 h) killing by either DAP or comparative prototypic cationic HDPs (hNP-1; LL-37). Multicolor flow cytometry was used to determine kinetic cell responses associated with resistance or susceptibility to these molecules. While overall DAP binding was similar between strains, a significant subpopulation of 351-D10 cells hyper-accumulated DAP (>2–4-fold vs. 351-WT). Further, both DAP and hNP-1 induced cell membrane (CM) hyper-polarization in 351-WT, corresponding to significantly greater temporal DAP-killing (vs. 351-D10). No strain-specific differences in CM permeabilization, lipid turnover or regulated cell death were observed post-exposure to DAP, hNP-1 or LL-37. Thus, the adaptive energetics of the CM appear coupled to the outcomes of interactions of S. mitis-oralis with DAP and selected HDPs. In contrast, altered CM permeabilization, proposed as a major mechanism of action of both DAP and HDPs, did not differentiate DAP-S vs. DAP-R phenotypes in this S. mitis-oralis strain-pair. Full article
(This article belongs to the Special Issue Antimicrobial Peptides and Host-Pathogen Interaction)
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16 pages, 2449 KiB  
Article
The Antimicrobial Peptide, Bactenecin 5, Supports Cell-Mediated but Not Humoral Immunity in the Context of a Mycobacterial Antigen Vaccine Model
by Tulika Munshi, Adam Sparrow, Brendan W. Wren, Rajko Reljic and Samuel J. Willcocks
Antibiotics 2020, 9(12), 926; https://doi.org/10.3390/antibiotics9120926 - 19 Dec 2020
Cited by 8 | Viewed by 2948
Abstract
Bactenecin (Bac) 5 is a bovine antimicrobial peptide (AMP) capable of killing some species of bacteria through the inhibition of protein synthesis. Bac5 and other AMPs have also been shown to have chemotactic properties and can induce inflammatory cytokine expression by innate immune [...] Read more.
Bactenecin (Bac) 5 is a bovine antimicrobial peptide (AMP) capable of killing some species of bacteria through the inhibition of protein synthesis. Bac5 and other AMPs have also been shown to have chemotactic properties and can induce inflammatory cytokine expression by innate immune cells. Recently, AMPs have begun to be investigated for their potential use as novel vaccine adjuvants. In the current work, we characterise the functionality of Bac5 in vitro using murine macrophage-like cells, ex vivo using human tonsil tissue and in vivo using a murine model of vaccination. We report the effects of the peptide in isolation and in the context of co-presentation with mycobacterial antigen and whole, inert Bacillus subtilis spore antigens. We find that Bac5 can trigger the release of nitric oxide from murine macrophages and upregulate surface marker expression including CD86, MHC-I and MHC-II, in the absence of additional agonists. When coupled with mycobacterial Ag85 and B. subtilis spores, Bac5 also enhanced IFNγ secretion. We provide evidence that B. subtilis spores, but not the Bac5 peptide, act as strong adjuvants in promoting antigen-specific immunoglobulin production in Ag85B-vaccinated mice. Our findings suggest that Bac5 is an important regulator of the early cell-mediated host immune response. Full article
(This article belongs to the Special Issue Antimicrobial Peptides and Host-Pathogen Interaction)
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15 pages, 7488 KiB  
Article
Improved Cell Selectivity of Pseudin-2 via Substitution in the Leucine-Zipper Motif: In Vitro and In Vivo Antifungal Activity
by Seong-Cheol Park, Heabin Kim, Jin-Young Kim, Hyeonseok Kim, Gang-Won Cheong, Jung Ro Lee and Mi-Kyeong Jang
Antibiotics 2020, 9(12), 921; https://doi.org/10.3390/antibiotics9120921 - 18 Dec 2020
Cited by 6 | Viewed by 3131
Abstract
Several antimicrobial peptides (AMPs) have been discovered, developed, and purified from natural sources and peptide engineering; however, the clinical applications of these AMPs are limited owing to their lack of abundance and side effects related to cytotoxicity, immunogenicity, and hemolytic activity. Accordingly, to [...] Read more.
Several antimicrobial peptides (AMPs) have been discovered, developed, and purified from natural sources and peptide engineering; however, the clinical applications of these AMPs are limited owing to their lack of abundance and side effects related to cytotoxicity, immunogenicity, and hemolytic activity. Accordingly, to improve cell selectivity for pseudin-2, an AMP from Pseudis paradoxa skin, in mammalian cells and pathogenic fungi, the sequence of pseudin-2 was modified by alanine or lysine at each position of two amino acids within the leucine-zipper motif. Alanine-substituted variants were highly selective toward fungi over HaCaT and erythrocytes and maintained their antifungal activities and mode of action (membranolysis). However, the antifungal activities of lysine-substituted peptides were reduced, and the compound could penetrate into fungal cells, followed by induction of mitochondrial reactive oxygen species and cell death. In vivo antifungal assays of analogous peptide showed excellent antifungal efficiency in a Candida tropicalis skin infection mouse model. Our results demonstrated the usefulness of selective amino acid substitution in the repeated sequence of the leucine-zipper motif for the design of AMPs with potent antimicrobial activities and low toxicity. Full article
(This article belongs to the Special Issue Antimicrobial Peptides and Host-Pathogen Interaction)
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