Candida albicans susceptibility to lactoperoxidase-generated hypoiodite

Ahariz, Mohamed; Courtois, Philippe

doi:10.2147/cciden.s10891

Cited by 11 publications

(3 citation statements)

References 17 publications

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“…In vitro , OI − decreases the survival rate of some microbial species at a lower concentration, as compared with that observed for OSCN − , especially in Candida albicans ( 79 ). Some authors ( 80 ) have been able to demonstrate that 125 I only binds to a limited number of membrane molecules of Candida albicans , which is particularly sensitive to OI − .…”

Section: Oxidant Production By Oral Peroxidasesmentioning

confidence: 67%

Oral peroxidases: From antimicrobial agents to ecological actors (Review)

Courtois

2021

Mol Med Rep

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Sialoperoxidase and myeloperoxidase are the two main peroxidase enzymes found in the oral cavity. Sialoperoxidase is present in salivary secretions and in the biofilms that line the oral surfaces, while myeloperoxidase is abundant in the dento-gingival sulcus area. In the presence of hydrogen peroxide (H 2 O 2 ), oral peroxidases catalyze the oxidation of the pseudohalide anion thiocyanate (SCN − ) to hypothiocyanite (OSCN − ), a strong oxidant that serves an antimicrobial role. Furthermore, oral peroxidases consume bacteria-produced H 2 O 2 and could help inactivate toxic carcinogenic and genotoxic substances. Numerous in vitro studies have reported the antibacterial, antimycotic and antiviral role of peroxidases, suggesting possible applications in oral therapy. However, the use of oral hygiene products incorporating peroxidase systems has not yet been shown to be beneficial for the treatment or prevention of oral infections. This paradox reflects our incomplete knowledge of the physiological role of peroxidases in a complex environment, such as the oral region. While hygiene is crucial for restoring oral microbiota to a symbiotic state, there are no data to suggest that the addition of a peroxidase per se can create a dysbiotic state. Recent investigations have associated the presence of peroxidase activity with gram-positive cocci microbial flora, and its insufficiency with dysbiosis has been linked to pathologies, such as caries, periodontitis or infections of the oral mucosa. Therefore, oxidants generated by oral peroxidases appear to be an essential ecological determinant for oral health through the selection of a symbiotic microbiota capable of resisting oxidative stress. The objective of the present review was to update the current knowledge of the physiological aspects and applications of oral peroxidases in clinical practice.

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Section: Oxidant Production By Oral Peroxidasesmentioning

confidence: 67%

Oral peroxidases: From antimicrobial agents to ecological actors (Review)

Courtois

2021

Mol Med Rep

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“…For example, Ihalin and group successively reported that the addition of SCN − into the peroxidase/H 2 O 2 /I − system abolished the bactericidal activity of the oxidized halide (Ihalin et al, 1998 , 2001 ). Similarly, Ahariz and Courtois ( 2010 ) demonstrated a competition between I − and SCN − , reporting that the addition of SCN − to peroxidase/G/GOD/I − system (G/GOD: glucose/glucose oxidase as source of hydrogen peroxide) decreased the antifungal effect of the system.…”

Section: Discussionmentioning

confidence: 89%

Antibacterial Potential of an Antimicrobial Agent Inspired by Peroxidase-Catalyzed Systems

et al. 2017

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Antibiotic resistance is an increasingly serious threat to global health. Consequently, the development of non-antibiotic based therapies and disinfectants, which avoid induction of resistance, or cross-resistance, is of high priority. We report the synthesis of a biocidal complex, which is produced by the reaction between ionic oxidizable salts—iodide and thiocyanate—in the presence of hydrogen peroxide as an oxidation source. The reaction generates bactericidal reactive oxygen and iodine species. In this study, we report that the iodo-thiocyanate complex (ITC) is an effective bactericidal agent with activity against planktonic and biofilm cells of Gram-negative (Escherichia coli and Pseudomonas aeruginosa) and Gram-positive (Staphylococcus aureus and methicillin-resistant S. aureus) bacteria. The minimum bactericidal concentrations and the minimum biofilm eradication concentrations of the biocidal composite were in the range of 7.8–31.3 and 31.3–250 μg ml−1, respectively. As a result, the complex was capable to cause a rapid cell death of planktonic test cultures at between 0.5 and 2 h, and complete eradication of dual and mono-species biofilms between 30 s and 10 min. Furthermore, the test bacteria, including a MRSA strain, exposed to the cocktail failed to develop resistance after serial passages. The antimicrobial activity of the ITC appears to derive from the combinational effect of the powerful species capable of oxidizing the essential biomolecules of bacteria. The use of this composition may provide an effective and efficient method for killing potential pathogens, as well as for disinfecting and removing biofilm contamination.

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“…These enzymes have antimicrobial and virucidal activities [ 8 , 23 , 24 , 25 , 26 , 27 , 28 ]. They are of interest and are used in various biomedical or biotechnological fields.…”

Section: Introductionmentioning

confidence: 99%

A Bacterial Myeloperoxidase with Antimicrobial Properties

Céré

Delord

Ymbe

et al. 2023

BioTech

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The four mammalian peroxidases (myeloperoxidase, eosinophilperoxidase, lactoperoxidase, and thyroid peroxidase) are widely studied in the literature. They catalyze the formation of antimicrobial compounds and participate in innate immunity. Owing to their properties, they are used in many biomedical, biotechnological, and agro-food applications. We decided to look for an enzyme that is easiest to produce and much more stable at 37 °C than mammalian peroxidases. To address this question, a peroxidase from Rhodopirellula baltica, identified by bioinformatics tools, was fully characterized in this study. In particular, a production and purification protocol including the study of heme reconstitution was developed. Several activity tests were also performed to validate the hypothesis that this peroxidase is a new homolog of mammalian myeloperoxidase. It has the same substrate specificities as the human one and accepts I−, SCN−, Br−, and Cl− as (pseudo-) halides. It also exhibits other auxiliary activities such as catalase and classical peroxidase activities, and it is very stable at 37 °C. Finally, this bacterial myeloperoxidase can kill the Escherichia coli strain ATCC25922, which is usually used to perform antibiograms.

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Candida albicans susceptibility to lactoperoxidase-generated hypoiodite

Cited by 11 publications

References 17 publications

Oral peroxidases: From antimicrobial agents to ecological actors (Review)

Oral peroxidases: From antimicrobial agents to ecological actors (Review)

Antibacterial Potential of an Antimicrobial Agent Inspired by Peroxidase-Catalyzed Systems

A Bacterial Myeloperoxidase with Antimicrobial Properties

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