Insights into the anticancer properties of the first antimicrobial peptide from Archaea

Gaglione, Rosa; Pirone, Luciano; Farina, Biancamaria; Fusco, Salvatore; Smaldone, Giovanni; Aulitto, Martina; Dell’Olmo, Eliana; Roscetto, Emanuela; Gatto, Annarita Del; Fattorusso, Roberto; Notomista, Eugenio; Zaccaro, Laura; Arciello, Angela; Pedone, Emilia; Contursi, Patrizia

doi:10.1016/j.bbagen.2017.06.009

Cited by 36 publications

(18 citation statements)

References 51 publications

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“…The isolation and characterization of extremophilic microorganisms has become a research hot topic in the last two decades (Horikoshi et al 2010;Turner et al 2007). For instance, (hyper)-thermophilic microorganisms have gained attention because they represent valuable sources of robust enzymes (Aulitto et al 2017a;Duffaud et al 1997;Naganagouda et al 2009) as well as of novel bioactive molecules (Gaglione et al 2017;Notomista et al 2015) that can be exploited for several biomedical and industrial applications (Elleuche et al 2015;Sarmiento et al 2015). As shown in this review, the growing concerns about the environmental impact of using chemical processes at industrial level has led to an increased interest in the development and/or optimisation of sustainable alternatives, which are based on the use of galactomannan-degrading enzymes as catalysts.…”

Section: Future Perspectivesmentioning

confidence: 99%

Galactomannan degradation by thermophilic enzymes: a hot topic for biotechnological applications

Aulitto

Fusco

Limauro

et al. 2019

World J Microbiol Biotechnol

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Extremophilic microorganisms are valuable sources of enzymes for various industrial applications. In fact, given their optimal catalytic activity and operational stability under harsh physical and chemical conditions, they represent a suitable alternative to their mesophilic counterparts. For instance, extremophilic enzymes are important to foster the switch from fossil-based to lignocellulose-based industrial processes. Indeed, more stable enzymes are needed, because the conversion of the lignocellulosic biomass to a wide palette of value-added products requires extreme chemo-physical pre-treatments. Galactomannans are part of the hemicellulose fraction in lignocellulosic biomass. They are heteropolymers constituted by a β-1,4-linked mannan backbone substituted with side chains of α-1,6-linked galactose residues. Therefore, the joint action of different hydrolytic enzymes (i.e. β-mannanase, β-mannosidase and α-galactosidase) is needed to accomplish their complete hydrolysis. So far, numerous galactomannan-degrading enzymes have been isolated and characterized from extremophilic microorganisms. Besides applications in biorefinery, these biocatalysts are also useful to improve the quality (i.e. digestibility and prebiotic properties) of food and feed as well as in paper industries to aid the pulp bleaching process. In this review, an overview about the structure, function and applications of galactomannans is provided. Moreover, a survey of (hyper)-thermophilic galactomannans-degrading enzymes, mainly characterized in the last decade, has been carried out. These extremozymes are described in the light of their biotechnological application in industrial processes requiring harsh conditions.

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Section: Future Perspectivesmentioning

confidence: 99%

Galactomannan degradation by thermophilic enzymes: a hot topic for biotechnological applications

Aulitto

Fusco

Limauro

et al. 2019

World J Microbiol Biotechnol

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“…The peptide was identified using an in silico tool developed to search for cryptic antimicrobial peptide-like sequences hidden in the primary structure of proteins 32 , 43 – 46 . VLL-28 displays chemical, physical and functional properties typical of CAMPs and acquires a defined structure in the presence of membrane mimetics 47 , 48 . Notably, this CAMP turned out to be toxic not only to Gram-negative and Gram-positive bacteria but also to C .…”

Section: Introductionmentioning

confidence: 99%

Antifungal and anti-biofilm activity of the first cryptic antimicrobial peptide from an archaeal protein against Candida spp. clinical isolates

Roscetto

Contursi

Vollaro

et al. 2018

Sci Rep

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Candida species cause cutaneous and systemic infections with a high mortality rate, especially in immunocompromised patients. The emergence of resistance to the most common antifungal drugs, also due to biofilm formation, requires the development of alternative antifungal agents. The antimicrobial peptide VLL-28, isolated from an archaeal transcription factor, shows comparable antifungal activity against 10 clinical isolates of Candida spp. Using a fluoresceinated derivative of this peptide, we found that VLL-28 binds to the surface of planktonic cells. This observation suggested that it could exert its antifungal activity by damaging the cell wall. In addition, analyses performed on biofilms via confocal microscopy revealed that VLL-28 is differentially active on all the strains tested, with C. albicans and C. parapsilosis being the most sensitive ones. Notably, VLL-28 is the first example of an archaeal antimicrobial peptide that is active towards Candida spp. Thus, this points to archaeal microorganisms as a possible reservoir of novel antifungal agents.

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“…Several researchers are involved in the design and evaluation of specific molecules with potential therapeutic use in chronic and biofilm-related infections [ 13 , 14 ]. In particular, antimicrobial peptides (AMPs), a small bioactive protein consisting of 12–50 amino acids, seem to have emerged as promising active agents against bacteria, viruses, fungi, and also as potential chemotherapeutic agents [ 15 , 16 , 17 , 18 ].…”

Section: Introductionmentioning

confidence: 99%

Anti-Biofilm Activity of the Fungal Phytotoxin Sphaeropsidin A against Clinical Isolates of Antibiotic-Resistant Bacteria

Roscetto

Masi²,

Esposito

et al. 2020

Toxins

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Many pathogens involved in human infection have rapidly increased their antibiotic resistance, reducing the effectiveness of therapies in recent decades. Most of them can form biofilms and effective drugs are not available to treat these formations. Natural products could represent an efficient solution in discovering and developing new drugs to overcome antimicrobial resistance and treat biofilm-related infections. In this study, 20 secondary metabolites produced by pathogenic fungi of forest plants and belonging to diverse classes of naturally occurring compounds were evaluated for the first time against clinical isolates of antibiotic-resistant Gram-negative and Gram-positive bacteria. epi-Epoformin, sphaeropsidone, and sphaeropsidin A showed antimicrobial activity on all test strains. In particular, sphaeropsidin A was effective at low concentrations with Minimum Inhibitory Concentration (MIC) values ranging from 6.25 μg/mL to 12.5 μg/mL against all reference and clinical test strains. Furthermore, sphaeropsidin A at sub-inhibitory concentrations decreased methicillin-resistant S. aureus (MRSA) and P. aeruginosa biofilm formation, as quantified by crystal violet staining. Interestingly, mixtures of sphaeropsidin A and epi-epoformin have shown antimicrobial synergistic effects with a concomitant reduction of cytotoxicity against human immortalized keratinocytes. Our data show that sphaeropsidin A and epi-epoformin possess promising antimicrobial properties.

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Insights into the anticancer properties of the first antimicrobial peptide from Archaea

Abstract: VLL-28 represents the first ACP identified in an archaeal microorganism, exerting a trans-kingdom activity.

Cited by 36 publications

References 51 publications

Galactomannan degradation by thermophilic enzymes: a hot topic for biotechnological applications

Galactomannan degradation by thermophilic enzymes: a hot topic for biotechnological applications

Antifungal and anti-biofilm activity of the first cryptic antimicrobial peptide from an archaeal protein against Candida spp. clinical isolates

Anti-Biofilm Activity of the Fungal Phytotoxin Sphaeropsidin A against Clinical Isolates of Antibiotic-Resistant Bacteria

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