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Antimicrobial peptides

About: Antimicrobial peptides is a research topic. Over the lifetime, 10645 publications have been published within this topic receiving 507688 citations. The topic is also known as: host defense peptide & antimicrobial protein.


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Journal ArticleDOI
TL;DR: This review will focus on expression, function, regulation and functional efficacy of antimicrobial peptides against F. nucleatum, one of the most interesting gram-negative bacteria implicated in periodontal diseases.
Abstract: The pathogenesis of periodontitis involves the interplay of microbiota present in the subgingival plaque and the host responses Inflammation and destruction of periodontal tissues are considered to result from the response of a susceptible host to a microbial biofilm containing gram-negative pathogens Antimicrobial peptides are important contributors to maintaining the balance between health and disease in this complex environment These include several salivary antimicrobial peptides such as β-defensins expressed in the epithelium and LL-37 expressed in both epithelium and neutrophils Among gram-negative bacteria implicated in periodontal diseases, Fusobacterium nucleatum, is one of the most interesting This review will focus on expression, function, regulation and functional efficacy of antimicrobial peptides against F nucleatum We are looking for how the presence of F nucleatum induces secretion of peptides which have an impact on host cells and modulate immune response

293 citations

Journal ArticleDOI
TL;DR: Although the Mj-AMPs show sequence similarity to mu-agatoxins, a class of insecticidal neurotoxic peptides isolated from the venom of spiders, they do not affect pulse transmission in insect nerves and exhibit a broad spectrum of antifungal activity.

293 citations

Journal ArticleDOI
TL;DR: The identification and characterization of a novel P. aeruginosa two-component regulator affecting polymyxin-adaptive resistance, ParR-ParS (PA1799-PA1798), which was required for activation of the arnBCADTEF LPS modification operon in the presence of subinhibitory concentrations of polymyXin, colistin, or the bovine peptide indolicidin, leading to increased resistance to various polycationic
Abstract: As multidrug resistance increases alarmingly, polymyxin B and colistin are increasingly being used in the clinic to treat serious Pseudomonas aeruginosa infections. In this opportunistic pathogen, subinhibitory levels of polymyxins and certain antimicrobial peptides induce resistance toward higher, otherwise lethal, levels of these antimicrobial agents. It is known that the modification of lipid A of lipopolysaccharide (LPS) is a key component of this adaptive peptide resistance, but to date, the regulatory mechanism underlying peptide regulation in P. aeruginosa has remained elusive. The PhoP-PhoQ and PmrA-PmrB two-component systems, which control this modification under low-Mg2+ conditions, do not appear to play a major role in peptide-mediated adaptive resistance, unlike in Salmonella where PhoQ is a peptide sensor. Here we describe the identification and characterization of a novel P. aeruginosa two-component regulator affecting polymyxin-adaptive resistance, ParR-ParS (PA1799-PA1798). This system was required for activation of the arnBCADTEF LPS modification operon in the presence of subinhibitory concentrations of polymyxin, colistin, or the bovine peptide indolicidin, leading to increased resistance to various polycationic antibiotics, including aminoglycosides. This study highlights the complexity of the regulatory network controlling resistance to cationic antibiotics and host peptides in P. aeruginosa, which has major relevance in the development and deployment of cationic antimicrobials.

293 citations

Journal ArticleDOI
TL;DR: This review addresses recent advances in the immunomodulatory activity of β-defensins as well as the involvement ofβ- defensins in fertility, development, wound healing and cancer.
Abstract: Defensins comprise one of the largest groups of host defence peptides, present throughout evolution, in fungi and flowering plants as well as in invertebrates and vertebrates. These cysteine-rich, cationic peptides have a common ability to kill a broad range of microorganisms including bacteria, yeast and viruses. As such, they are a strong component of the arsenal that is an organism's innate immunity. It is becoming increasingly clear, however, that antimicrobial action is only one of the numerous roles of these multifunctional peptides. In recent years, the functions of defensins in immunomodulation have been widely investigated, and their involvement in other processes (such as fertility) is becoming evident. This review addresses recent advances in the immunomodulatory activity of β-defensins as well as the involvement of β-defensins in fertility, development, wound healing and cancer.

292 citations

Journal ArticleDOI
Jr Laszlo Otvos1
TL;DR: Careful selection of lead molecules based on the insect antibacterial peptides may extend their utility and produce viable alternatives to the conventional antimicrobial compounds for mammalian therapy.
Abstract: Insects are amazingly resistant to bacterial infections. To combat pathogens, insects rely on cellular and humoral mechanisms, innate immunity being dominant in the latter category. Upon detection of bacteria, a complex genetic cascade is activated, which ultimately results in the synthesis of a battery of antibacterial peptides and their release into the haemolymph. The peptides are usually basic in character and are composed of 20-40 amino acid residues, although some smaller proteins are also included in the antimicrobial repertoire. While the proline-rich peptides and the glycine-rich peptides are predominantly active against Gram-negative strains, the defensins selectively kill Gram-positive bacteria and the cecropins are active against both types. The insect antibacterial peptides are very potent: their IC50 (50% of the bacterial growth inhibition) hovers in the submicromolar or low micromolar range. The majority of the peptides act through disintegrating the bacterial membrane or interfering with membrane assembly, with the exception of drosocin, apidaecin and pyrrhocoricin which appear to deactivate a bacterial protein in a stereospecific manner. In accordance with their biological function, the membrane-active peptides form ordered structures, e.g. alpha-helices or beta-pleated sheets and often cast permeable ion-pores. Their cytotoxic properties were exploited in in vivo studies targeting tumour progression. Although the native peptides degrade quickly in biological fluids other than insect haemolymph, structural modifications render the peptides resistant against proteases without sacrificing biological activity. Indeed, a pyrrhocoricin analogue shows lack of toxicity in vitro and in vivo and protects mice against experimental Escherichia coli infection. Careful selection of lead molecules based on the insect antibacterial peptides may extend their utility and produce viable alternatives to the conventional antimicrobial compounds for mammalian therapy.

291 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023512
20221,025
2021809
2020844
2019728
2018634