The secrets of dermcidin action

Burian, Marc; Schittek, Birgit

doi:10.1016/j.ijmm.2014.12.012

Cited by 51 publications

(42 citation statements)

References 26 publications

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“…However, this paradigm has been recently challenged with the concept of "trained immunity" [14] , and the demonstration of memory responses of natural killer (NK) cells and innate lymphoid cells (ILCs) [ 15-17 ; for a review, see 18 ]. At host-environment contact interfaces, such as the skin, the gut or the airways, microbial stimuli initially elicit the secretion of generic antimicrobial peptides (AMPs, such as defensins or cathelicidin/ LL-37) as well as organ-specific mediators (such as dermcidin for the skin [19,20] ). Innate immune PRRs, prototypically TLRs [21,22] , expressed by resident (epithelial) or recruited (hematopoietic) cells, sense pathogen-associated molecular patterns (PAMPs) or, in the case of nonpathogenic microbes, more broadly termed "microbe-associated molecular patterns" (MAMPs), and trigger downstream effector programs.…”

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confidence: 99%

Cellular Innate Immunity: An Old Game with New Players

et al. 2016

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Innate immunity is a rapidly evolving field with novel cell types and molecular pathways being discovered and paradigms changing continuously. Innate and adaptive immune responses are traditionally viewed as separate from each other, but emerging evidence suggests that they overlap and mutually interact. Recently discovered cell types, particularly innate lymphoid cells and myeloid-derived suppressor cells, are gaining increasing attention. Here, we summarize and highlight current concepts in the field, focusing on innate immune cells as well as the inflammasome and DNA sensing which appear to be critical for the activation and orchestration of innate immunity, and may provide novel therapeutic opportunities for treating autoimmune, autoinflammatory, and infectious diseases.

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confidence: 99%

Cellular Innate Immunity: An Old Game with New Players

et al. 2016

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“…After an initial binding step when the cationic N-terminal region is electrostatically attracted by negatively charged PLs, the peptide eventually forms oligomeric channels stabilized by zinc ions in the membrane. Recently, three functional models and channel structures have been proposed: (i) the positive N-termini of the peptide molecules are embedded in the membrane with the negative C-termini floating on the surface, (ii) the cationic N-terminal regions of the peptides are folded back to the C-terminal regions forming transmembrane hairpins, and (iii) the peptides are tilted enough to maintain the channel completely in the membrane ( Figure 1B) (23,42,43).…”

Section: Interactions Of Anionic Amps With Microbial Membranesmentioning

confidence: 99%

“…One can hypothesize that anionic AMPs have evolved in response to such resistant microorganisms. However, when one takes into account the proposed models of interactions of α-helical dermcidin-derived peptides with microbial membranes (23), which postulate an important role of the cationic N-terminus in initial binding, the emerging picture of the interactions between anionic AMPs and microbial cells appears to be much more complicated. On the other hand, recently Prabhu et al (44) have characterized the first anionic defense peptide (isolated from plant Cocos nucifera) exhibiting antiproliferative activity against human glioma cell lines.…”

Section: Interactions Of Anionic Amps With Microbial Membranesmentioning

confidence: 99%

“…Haversen et al (107) showed that a 14-amino acid fragment from the N-terminus of human lactoferrin was highly active against E. coli, S. aureus, and C. albicans. Interestingly, it was found that the optimal length for the antimicrobial activity of the lactoferrinderived sequence is 12 aa (amino acids 19-31), but 13 aa (amino acids [17][18][19][20][21][22][23][24][25][26][27][28][29][30] was optimal for amebicidal properties (108)(109)(110). Recently, a new strategy to identify putative AMPs encrypted in protein sequences has been described.…”

Section: Natural Amp-derived Fragments and Design Of Hybrid Peptidesmentioning

confidence: 99%

“…Galleria mellonella defensins and a cecropin D-like peptide, or even highly anionic ones, e.g. G. mellonella anionic peptide 1 and 2, some insect and amphibian defensins, amphibian maximin 5, and human dermcidin (21)(22)(23)(24)(25).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Defense peptides: recent developments

Cytryńska

Zdybicka-Barabas

2015

Biomolecular Concepts

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Defense peptides are small amphipathic molecules that exhibit antimicrobial, antitumor, antiviral, and immunomodulatory properties. This review summarizes current knowledge on the mechanisms of antimicrobial activity of cationic and anionic defense peptides, indicating peptide-based as well as microbial cell-based factors affecting this activity. The peptide-based factors include charge, hydrophibicity, and amphipathicity, whereas the pathogen-based factors are membrane lipid composition, presence of sterols, membrane fluidity, cell wall components, and secreted factors such as extracellular proteinases. Since defense peptides have been considered very promising molecules that could replace conventional antibiotics in the era of drug-resistant pathogens, the issue of microbial resistance to antimicrobial peptides (AMPs) is addressed. Furthermore, selected approaches employed for optimization and de novo design of effective AMPs based on the properties recognized as important for the function of natural defense peptides are presented.

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A review on anti‐tuberculosis peptides: Impact of peptide structure on anti‐tuberculosis activity

Yathursan

Wiles

Read

et al. 2019

Journal of Peptide Science

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Antibiotic resistance is a major public health problem globally. Particularly concerning amongst drug‐resistant human pathogens is Mycobacterium tuberculosis that causes the deadly infectious tuberculosis (TB) disease. Significant issues associated with current treatment options for drug‐resistant TB and the high rate of mortality from the disease makes the development of novel treatment options against this pathogen an urgent need. Antimicrobial peptides are part of innate immunity in all forms of life and could provide a potential solution against drug‐resistant TB. This review is a critical analysis of antimicrobial peptides that are reported to be active against the M tuberculosis complex exclusively. However, activity on non‐TB strains such as Mycobacterium avium and Mycobacterium intracellulare, whenever available, have been included at appropriate sections for these anti‐TB peptides. Natural and synthetic antimicrobial peptides of diverse sequences, along with their chemical structures, are presented, discussed, and correlated to their observed antimycobacterial activities. Critical analyses of the structure allied to the anti‐mycobacterial activity have allowed us to draw important conclusions and ideas for research and development on these promising molecules to realise their full potential. Even though the review is focussed on peptides, we have briefly summarised the structures and potency of the various small molecule drugs that are available and under development, for TB treatment.

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The secrets of dermcidin action

Cited by 51 publications

References 26 publications

Cellular Innate Immunity: An Old Game with New Players

Cellular Innate Immunity: An Old Game with New Players

Defense peptides: recent developments

A review on anti‐tuberculosis peptides: Impact of peptide structure on anti‐tuberculosis activity

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