Hedistin: A novel antimicrobial peptide containing bromotryptophan constitutively expressed in the NK cells-like of the marine annelid, Nereis diversicolor

Tasiemski, Aurélie; Schikorski, David; Marrec-Croq, Françoise Le; Camp, Christelle Pontoire-Van; Boidin-Wichlacz, Céline; Sautière, Pierre-Éric

doi:10.1016/j.dci.2006.11.003

Cited by 73 publications

(54 citation statements)

References 31 publications

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“…The best characterized of these AMPs is styelin D, which possesses α-helical structure and is highly unusual in that it contains twelve post-translationally modified residues [77]. For example, the peptide contained multiple bromotryptophan residues, which are found in the AMPs of other marine organisms [218,219,220,221,222] and play an important role in the life of sea sponges and lower marine invertebrates [223]. Styelin D’s post-translationally modified residues enhanced the peptide’s membranolytic action at low pH but only against Gram-positive bacteria.…”

Section: An Overview Of Ph Dependent Peptides and Proteins With Anmentioning

confidence: 99%

pH Dependent Antimicrobial Peptides and Proteins, Their Mechanisms of Action and Potential as Therapeutic Agents

et al. 2016

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Antimicrobial peptides (AMPs) are potent antibiotics of the innate immune system that have been extensively investigated as a potential solution to the global problem of infectious diseases caused by pathogenic microbes. A group of AMPs that are increasingly being reported are those that utilise pH dependent antimicrobial mechanisms, and here we review research into this area. This review shows that these antimicrobial molecules are produced by a diverse spectrum of creatures, including vertebrates and invertebrates, and are primarily cationic, although a number of anionic examples are known. Some of these molecules exhibit high pH optima for their antimicrobial activity but in most cases, these AMPs show activity against microbes that present low pH optima, which reflects the acidic pH generally found at their sites of action, particularly the skin. The modes of action used by these molecules are based on a number of major structure/function relationships, which include metal ion binding, changes to net charge and conformational plasticity, and primarily involve the protonation of histidine, aspartic acid and glutamic acid residues at low pH. The pH dependent activity of pore forming antimicrobial proteins involves mechanisms that generally differ fundamentally to those used by pH dependent AMPs, which can be described by the carpet, toroidal pore and barrel-stave pore models of membrane interaction. A number of pH dependent AMPs and antimicrobial proteins have been developed for medical purposes and have successfully completed clinical trials, including kappacins, LL-37, histatins and lactoferrin, along with a number of their derivatives. Major examples of the therapeutic application of these antimicrobial molecules include wound healing as well as the treatment of multiple cancers and infections due to viruses, bacteria and fungi. In general, these applications involve topical administration, such as the use of mouth washes, cream formulations and hydrogel delivery systems. Nonetheless, many pH dependent AMPs and antimicrobial proteins have yet to be fully characterized and these molecules, as a whole, represent an untapped source of novel biologically active agents that could aid fulfillment of the urgent need for alternatives to conventional antibiotics, helping to avert a return to the pre-antibiotic era.

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Section: An Overview Of Ph Dependent Peptides and Proteins With Anmentioning

confidence: 99%

pH Dependent Antimicrobial Peptides and Proteins, Their Mechanisms of Action and Potential as Therapeutic Agents

et al. 2016

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“…As one of the most vital defense components, antimicrobial peptides are now considered as one of the universal host defense tools of living organisms against microbial infection. Up to now, the molecular weight of antibacterial peptides are generally found to be below 60 KDa (Tasiemski et al, 2007). In this study we described the isolation and purification of an earthworm protein from coelomic fluid (ECFP) with the approximate molecular weight of 38.6 KDa.…”

Section: Discussionmentioning

confidence: 99%

Purification of a protein from coelomic fluid of the earthworm Eisenia foetida and evaluation of its hemolytic, antibacterial, and antitumor activities

Zhang

Wang

Cao

et al. 2011

Pharmaceutical Biology

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“…The residue Trp2 in the sequence of styelin D from sea squirt was brominated at position 6 of the aromatic ring. A similar modification might exist in cathelicidins from hagfish, hedistin, and centrocins [19][20][21]. A synthetic hedistin analog without bromination was found to be as active as the modified natural form, indicating bromination is not critical for antimicrobial activity [20].…”

Section: Halogenation (Br or Cl)mentioning

confidence: 99%

“…A similar modification might exist in cathelicidins from hagfish, hedistin, and centrocins [19][20][21]. A synthetic hedistin analog without bromination was found to be as active as the modified natural form, indicating bromination is not critical for antimicrobial activity [20]. In lantibiotic Microbisporicin A1, Trp4 is unprecedentedly chlorinated at position 5 [22].…”

Section: Halogenation (Br or Cl)mentioning

confidence: 99%

Post-Translational Modifications of Natural Antimicrobial Peptides and Strategies for Peptide Engineering

Wang¹

2011

CBIOT

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Natural antimicrobial peptides (AMPs) are gene-coded defense molecules discovered in all the three life domains: Eubacteria, Archaea, and Eukarya. The latter covers protists, fungi, plants, and animals. It is now recognized that amino acid composition, peptide sequence, and posttranslational modifications determine to a large extent the structure and function of AMPs. This article systematically describes post-translational modifications of natural AMPs annotated in the antimicrobial peptide database (http://aps.unmc.edu/AP). Currently, 1147 out of 1755 AMPs in the database are modified and classified into more than 17 types. Through chemical modifications, the peptides fold into a variety of structural scaffolds that target bacterial surfaces or molecules within cells. Chemical modifications also confer desired functions to a particular peptide. Meanwhile, these modifications modulate other peptide properties such as stability. Elucidation of the relationship between AMP property and chemical modification inspires peptide engineering. Depending on the objective of our design, peptides may be modified in various ways so that the desired features can be enhanced whereas unwanted properties can be minimized. Therefore, peptide design plays an essential role in developing natural AMPs into a new generation of therapeutic molecules.

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Hedistin: A novel antimicrobial peptide containing bromotryptophan constitutively expressed in the NK cells-like of the marine annelid, Nereis diversicolor

Cited by 73 publications

References 31 publications

pH Dependent Antimicrobial Peptides and Proteins, Their Mechanisms of Action and Potential as Therapeutic Agents

pH Dependent Antimicrobial Peptides and Proteins, Their Mechanisms of Action and Potential as Therapeutic Agents

Purification of a protein from coelomic fluid of the earthworm Eisenia foetida and evaluation of its hemolytic, antibacterial, and antitumor activities

Post-Translational Modifications of Natural Antimicrobial Peptides and Strategies for Peptide Engineering

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