Identification of a Novel Antifungal Peptide with Chitin-Binding Property from Marine Metagenome

Muthuirulan, Pushpanathan; Rajendhran, Jeyaprakash; Jayashree, S.; Sundarakrishnan, Balakrishnan; Jayachandran, S; Gunasekaran, Paramasamy

doi:10.2174/092986612803521620

Cited by 32 publications

(24 citation statements)

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“…It predicted α-helical conformation with an extended coil containing an N -acetyl- d -glucosamine binding site which was demonstrated by circular dichroism spectroscopy in the presence of chitin or the membrane mimicking solvent, trifluoroethanol. Its chitin-binding activity was corroborated by fast-performance liquid chromatography (Pushpanathan et al 2012). …”

Section: Antifungal Productsmentioning

confidence: 98%

Antifungal and antiviral products of marine organisms

Cheung

Wong

Pan

et al. 2014

Appl Microbiol Biotechnol

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Marine organisms including bacteria, fungi, algae, sponges, echinoderms, mollusks, and cephalochordates produce a variety of products with antifungal activity including bacterial chitinases, lipopeptides, and lactones; fungal (−)-sclerotiorin and peptaibols, purpurides B and C, berkedrimane B and purpuride; algal gambieric acids A and B, phlorotannins; 3,5-dibromo-2-(3,5-dibromo-2-methoxyphenoxy)phenol, spongistatin 1, eurysterols A and B, nortetillapyrone, bromotyrosine alkaloids, bis-indole alkaloid, ageloxime B and (−)-ageloxime D, haliscosamine, hamigeran G, hippolachnin A from sponges; echinoderm triterpene glycosides and alkene sulfates; molluscan kahalalide F and a 1485-Da peptide with a sequence SRSELIVHQR; and cepalochordate chitotriosidase and a 5026.9-Da antifungal peptide. The antiviral compounds from marine organisms include bacterial polysaccharide and furan-2-yl acetate; fungal macrolide, purpurester A, purpurquinone B, isoindolone derivatives, alterporriol Q, tetrahydroaltersolanol C and asperterrestide A, algal diterpenes, xylogalactofucan, alginic acid, glycolipid sulfoquinovosyldiacylglycerol, sulfated polysaccharide p-KG03, meroditerpenoids, methyl ester derivative of vatomaric acid, lectins, polysaccharides, tannins, cnidarian zoanthoxanthin alkaloids, norditerpenoid and capilloquinol; crustacean antilipopolysaccharide factors, molluscan hemocyanin; echinoderm triterpenoid glycosides; tunicate didemnin B, tamandarins A and B and; tilapia hepcidin 1–5 (TH 1–5), seabream SauMx1, SauMx2, and SauMx3, and orange-spotted grouper β-defensin. Although the mechanisms of antifungal and antiviral activities of only some of the afore-mentioned compounds have been elucidated, the possibility to use those known to have distinctly different mechanisms, good bioavailability, and minimal toxicity in combination therapy remains to be investigated. It is also worthwhile to test the marine antimicrobials for possible synergism with existing drugs. The prospects of employing them in clinical practice are promising in view of the wealth of these compounds from marine organisms. The compounds may also be used in agriculture and the food industry.

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Section: Antifungal Productsmentioning

confidence: 98%

Antifungal and antiviral products of marine organisms

Cheung

Wong

Pan

et al. 2014

Appl Microbiol Biotechnol

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“…However, bacterial membrane and fungi cell wall have different contents. For example, chitin is one of the major components of fungal cell walls and some of antifungal peptides are capable of binding to chitin [91,92,93]. Such binding ability helps AMPs to target fungal cells efficiently.…”

Section: Major Categories Of Amps and Mechanisms Of Actionmentioning

confidence: 99%

Antimicrobial Peptides

2013

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The rapid increase in drug-resistant infections has presented a serious challenge to antimicrobial therapies. The failure of the most potent antibiotics to kill “superbugs” emphasizes the urgent need to develop other control agents. Here we review the history and new development of antimicrobial peptides (AMPs), a growing class of natural and synthetic peptides with a wide spectrum of targets including viruses, bacteria, fungi, and parasites. We summarize the major types of AMPs, their modes of action, and the common mechanisms of AMP resistance. In addition, we discuss the principles for designing effective AMPs and the potential of using AMPs to control biofilms (multicellular structures of bacteria embedded in extracellular matrixes) and persister cells (dormant phenotypic variants of bacterial cells that are highly tolerant to antibiotics).

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“…albicans and 4.29 µM for A. niger [13,14]. The mechanism of action this peptide in exhibiting antifungal activity remains unexplored.…”

Section: Introductionmentioning

confidence: 99%

Mechanisms of the Antifungal Action of Marine Metagenome-Derived Peptide, MMGP1, against Candida albicans

2013

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BackgroundDevelopment of resistant variants to existing antifungal drugs continues to be the serious problem in Candida albicans-induced fungal pathogenesis, which has a considerable impact on animal and human health. Identification and characterization of newer drugs against C. albicans is, therefore, essential. MMGP1 is a direct cell-penetrating peptide recently identified from marine metagenome, which was found to possess potent antifungal activity against C. albicans.Methodology/Principal FindingsIn this study, we investigated the mechanism of antifungal action of MMGP1 against C. albicans. Agarose gel shift assay found the peptide to be having a remarkable DNA-binding ability. The modification of the absorption spectra and fluorescence quenching of the tryptophyl residue correspond to the stacking between indole ring and nucleotide bases. The formation of peptide–DNA complexes was confirmed by fluorescence quenching of SYTO 9 probe. The interaction of peptide with plasmid DNA afforded protection of DNA from enzymatic degradation by DNase I. In vitro transcription of mouse β-actin gene in the presence of peptide led to a decrease in the level of mRNA synthesis. The C. albicans treated with MMGP1 showed strong inhibition of biosynthetic incorporation of uridine analog 5-ethynyluridine (EU) into nascent RNA, suggesting the peptide’s role in the inhibition of macromolecular synthesis. Furthermore, the peptide also induces endogenous accumulation of reactive oxygen species (ROS) in C. albicans. MMGP1 supplemented with glutathione showed an increased viability of C. albicans cells. The hyper-produced ROS by MMGP1 leads to increased levels of protein carbonyls and thiobarbituric acid reactive substances and it also causes dissipation of mitochondrial membrane potential and DNA fragmentation in C. albicans cells.Conclusion And Significance: Therefore, the antifungal activity of MMGP1 could be attributed to its binding with DNA, causing inhibition of transcription followed by endogenous production of ROS, which triggers cascade of events that leads to cell death.

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Identification of a Novel Antifungal Peptide with Chitin-Binding Property from Marine Metagenome

Cited by 32 publications

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Antifungal and antiviral products of marine organisms

Antifungal and antiviral products of marine organisms

Antimicrobial Peptides

Mechanisms of the Antifungal Action of Marine Metagenome-Derived Peptide, MMGP1, against Candida albicans

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