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Antimicrobial Peptides and Antimicrobial Chemokines 2.0

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pathology, Diagnostics, and Therapeutics".

Deadline for manuscript submissions: closed (31 August 2022) | Viewed by 7525

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Istituto Superiore di Sanita’, National Centre for Pre-Clinical and Clinical Drug Research and Evaluation, Pharmacological Research and Experimental Therapy Unit, 00166 Rome, Italy
Interests: psoriasis; antimicrobial peptides; immunology and microbiology medicine biochemistry, genetics and molecular biology chemistry physics and astronomy engineering materials science environmental science pharmacology, toxicology and pharmaceutics
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Special Issue Information

Dear Colleagues,

Antimicrobial peptides (AMPs) are natural antibiotics produced by epithelial cells or immune cells, and are active against viruses, bacteria and fungi. They are generally cationic, with hydrophobic residues making the folded peptide able to kill pathogens. However, AMPs also have pleiotropic effector functions which act on various cell types, including the cells of the immune system. Given the capacity to induce/regulate inflammatory pathways, some AMPs, such as cathelicidin LL37 or defensins, play a pathogenic role in autoimmune/auto-inflammatory diseases, such as psoriasis or systemic lupus erythematosus. Interestingly, antimicrobial chemokines also exist and can demonstrate similar structures, cationicities and functions. Several investigators have discovered various chemokines (for instance, CXCL7, CXCL10, CXCL4, CXCL6, CCL20) with antimicrobial properties. Among these, CXCL4 and CXCL10 are up-regulated in some autoimmune conditions, and CXCL4 mediates immune amplification in systemic sclerosis. Like the AMPs, antimicrobial chemokines can show a plethora of effector functions which act between antimicrobial activity and inflammation. Improving our understanding of the AMPs/anti-microbial chemokines effects in autoimmunity helps the identification of new biomarkers and therapy targets.

This Special Issue calls for original research papers and reviews on the molecular mechanisms underlying AMPs/antimicrobial chemokines’ involvement in the pathogenesis of human autoimmune/auto-inflammatory diseases. Appropriate animal studies on chronic disease models are also of interest.

Dr. Loredana Frasca
Guest Editor

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Keywords

  • antimicrobial peptides
  • antimicrobial chemokines
  • chronic inflammatory diseases
  • autoimmunity
  • biomarkers
  • therapy targets
  • inflammation
  • immune regulation
  • innate immunity
  • adaptive immunity

Published Papers (4 papers)

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Research

15 pages, 2886 KiB  
Article
CXCL4-RNA Complexes Circulate in Systemic Sclerosis and Amplify Inflammatory/Pro-Fibrotic Responses by Myeloid Dendritic Cells
by Immacolata Pietraforte, Alessia Butera, Lucia Gaddini, Anna Mennella, Raffaella Palazzo, Doriana Campanile, Katia Stefanantoni, Valeria Riccieri, Roberto Lande and Loredana Frasca
Int. J. Mol. Sci. 2023, 24(1), 653; https://doi.org/10.3390/ijms24010653 - 30 Dec 2022
Cited by 6 | Viewed by 1713
Abstract
CXCL4 is an important biomarker of systemic sclerosis (SSc), an incurable autoimmune disease characterized by vasculopathy and skin/internal organs fibrosis. CXCL4 contributes to the type I interferon (IFN-I) signature, typical of at least half of SSc patients, and its presence is linked to [...] Read more.
CXCL4 is an important biomarker of systemic sclerosis (SSc), an incurable autoimmune disease characterized by vasculopathy and skin/internal organs fibrosis. CXCL4 contributes to the type I interferon (IFN-I) signature, typical of at least half of SSc patients, and its presence is linked to an unfavorable prognosis. The mechanism implicated is CXCL4 binding to self-DNA, with the formation of complexes amplifying TLR9 stimulation in plasmacytoid dendritic cells (pDCs). Here, we demonstrate that, upon binding to self-RNA, CXCL4 protects the RNA from enzymatic degradation. As a consequence, CXCL4-RNA complexes persist in vivo. Indeed, we show for the first time that CXCL4-RNA complexes circulate in SSc plasma and correlate with both IFN-I and TNF-α. By using monocyte-derived DCs (MDDCs) pretreated with IFN-α as a model system (to mimic the SSc milieu of the IFN-I signature), we demonstrate that CXCL4-RNA complexes induce MDDC maturation and increase, in particular, pro-inflammatory TNF-α as well as IL-12, IL-23, IL-8, and pro-collagen, mainly in a TLR7/8-dependent but CXCR3-independent manner. In contrast, MDDCs produced IL-6 and fibronectin independently in their CXCL4 RNA-binding ability. These findings support a role for CXCL4-RNA complexes, besides CXCL4-DNA complexes, in immune amplification via the modulation of myeloid DC effector functions in SSc and also during normal immune responses. Full article
(This article belongs to the Special Issue Antimicrobial Peptides and Antimicrobial Chemokines 2.0)
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14 pages, 2456 KiB  
Article
Semi-Biosynthetic Production of Surface-Binding Adhesive Antimicrobial Peptides Using Intein-Mediated Protein Ligation
by Young Eun Hwang, Seonghun Im, Ju Hyun Cho, Wonsik Lee, Byung-Kwan Cho, Bong Hyun Sung and Sun Chang Kim
Int. J. Mol. Sci. 2022, 23(23), 15202; https://doi.org/10.3390/ijms232315202 - 02 Dec 2022
Cited by 1 | Viewed by 1573
Abstract
Microbial infections remain a global health concern, calling for the urgent need to implement effective prevention measures. Antimicrobial peptides (AMPs) have been extensively studied as potential antimicrobial coating agents. However, an efficient and economical method for AMP production is lacking. Here, we synthesized [...] Read more.
Microbial infections remain a global health concern, calling for the urgent need to implement effective prevention measures. Antimicrobial peptides (AMPs) have been extensively studied as potential antimicrobial coating agents. However, an efficient and economical method for AMP production is lacking. Here, we synthesized the direct coating adhesive AMP, NKC-DOPA5, composed of NKC, a potent AMP, and repeats of the adhesive amino acid 3,4-dihydroxyphenylalanine (DOPA) via an intein-mediated protein ligation strategy. NKC was expressed as a soluble fusion protein His-NKC-GyrA (HNG) in Escherichia coli, comprising an N-terminal 6× His-tag and a C-terminal Mxe GyrA intein. The HNG protein was efficiently produced in a 500-L fermenter, with a titer of 1.63 g/L. The NKC-thioester was released from the purified HNG fusion protein by thiol attack and subsequently ligated with chemically synthesized Cys-DOPA5. The ligated peptide His-NKC-Cys-DOPA5 was obtained at a yield of 88.7%. The purified His-NKC-Cys-DOPA5 possessed surface-binding and antimicrobial properties identical to those of the peptide obtained via solid-phase peptide synthesis. His-NKC-Cys-DOPA5 can be applied as a practical and functional antimicrobial coating to various materials, such as medical devices and home appliances. Full article
(This article belongs to the Special Issue Antimicrobial Peptides and Antimicrobial Chemokines 2.0)
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13 pages, 4346 KiB  
Article
Residual Interactions of LL-37 with POPC and POPE:POPG Bilayer Model Studied by All-Atom Molecular Dynamics Simulation
by Muhammad Yusuf, Wanda Destiarani, Ade Rizqi Ridwan Firdaus, Fauzian Giansyah Rohmatulloh, Mia Tria Novianti, Gita Widya Pradini and Reiva Farah Dwiyana
Int. J. Mol. Sci. 2022, 23(21), 13413; https://doi.org/10.3390/ijms232113413 - 02 Nov 2022
Cited by 1 | Viewed by 1695
Abstract
LL-37 is a membrane-active antimicrobial peptide (AMP) that could disrupt the integrity of bacterial membranes due to its inherent cationic and amphipathic nature. Developing a shorter derivative of a long peptide such as LL-37 is of great interest, as it can reduce production [...] Read more.
LL-37 is a membrane-active antimicrobial peptide (AMP) that could disrupt the integrity of bacterial membranes due to its inherent cationic and amphipathic nature. Developing a shorter derivative of a long peptide such as LL-37 is of great interest, as it can reduce production costs and cytotoxicity. However, more detailed information about the residual interaction between LL-37 and the membrane is required for further optimization. Previously, molecular dynamics simulation using mixed all-atom and united-atom force fields showed that LL-37 could penetrate the bilayer membrane. This study aimed to perform all-atom molecular dynamics simulations, highlighting the residual interaction of LL-37 with the simplest model of the bacterial membrane, POPE:POPG (2:1), and compare its interaction with the POPC, which represents the eukaryotic membrane. The result showed leucine–leucine as the leading residues of LL-37 that first contact the membrane surface. Then, the cationic peptide of LL-37 started to penetrate the membrane by developing salt bridges between positively charged amino acids, Lys–Arg, and the exposed phosphate group of POPE:POPG, which is shielded in POPC. Residues 18 to 29 are suggested as the core region of LL-37, as they actively interact with the POPE:POPG membrane, not POPC. These results could provide a basis for modifying the amino acid sequence of LL-37 and developing a more efficient design for LL-37 derivatives. Full article
(This article belongs to the Special Issue Antimicrobial Peptides and Antimicrobial Chemokines 2.0)
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23 pages, 5211 KiB  
Article
Systematic Screening of Penetratin’s Protein Targets by Yeast Proteome Microarrays
by Pramod Shah and Chien-Sheng Chen
Int. J. Mol. Sci. 2022, 23(2), 712; https://doi.org/10.3390/ijms23020712 - 10 Jan 2022
Cited by 3 | Viewed by 1885
Abstract
Cell-penetrating peptides (CPPs) have distinct properties to translocate across cell envelope. The key property of CPPs to translocation with attached molecules has been utilized as vehicles for the delivery of several potential drug candidates that illustrate the significant effect in in-vitro experiment but [...] Read more.
Cell-penetrating peptides (CPPs) have distinct properties to translocate across cell envelope. The key property of CPPs to translocation with attached molecules has been utilized as vehicles for the delivery of several potential drug candidates that illustrate the significant effect in in-vitro experiment but fail in in-vivo experiment due to selectively permeable nature of cell envelop. Penetratin, a well-known CPP identified from the third α-helix of Antennapedia homeodomain of Drosophila, has been widely used and studied for the delivery of bioactive molecules to treat cancers, stroke, and infections caused by pathogenic organisms. Few studies have demonstrated that penetratin directly possesses antimicrobial activities against bacterial and fungal pathogens; however, the mechanism is unknown. In this study, we have utilized the power of high-throughput Saccharomyces cerevisiae proteome microarrays to screen all the potential protein targets of penetratin. Saccharomyces cerevisiae proteome microarrays assays of penetratin followed by statistical analysis depicted 123 Saccharomyces cerevisiae proteins as the protein targets of penetratin out of ~5800 Saccharomyces cerevisiae proteins. To understand the target patterns of penetratin, enrichment analyses were conducted using 123 protein targets. In biological process: ribonucleoprotein complex biogenesis, nucleic acid metabolic process, actin filament-based process, transcription, DNA-templated, and negative regulation of gene expression are a few significantly enriched terms. Cytoplasm, nucleus, and cell-organelles are enriched terms for cellular component. Protein-protein interactions network depicted ribonucleoprotein complex biogenesis, cortical cytoskeleton, and histone binding, which represent the major enriched terms for the 123 protein targets of penetratin. We also compared the protein targets of penetratin and intracellular protein targets of antifungal AMPs (Lfcin B, Histatin-5, and Sub-5). The comparison results showed few unique proteins between penetratin and AMPs. Nucleic acid metabolic process and cellular component disassembly were the common enrichment terms for penetratin and three AMPs. Penetratin shows unique enrichment items that are related to DNA biological process. Moreover, motif enrichment analysis depicted different enriched motifs in the protein targets of penetratin, LfcinB, Histatin-5, and Sub-5. Full article
(This article belongs to the Special Issue Antimicrobial Peptides and Antimicrobial Chemokines 2.0)
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