Myeloperoxidase (MPO) and eosinophil peroxidase (EPO) provide the basis for safe, broad-spectrum microbicidal agents against serious and resistant infections.

MPO and EPO are enzymes that play a central role in the immune system’s defense against infection. More specifically, these enzymes catalyze the oxidation of halide by hydrogen peroxide to form reactive oxygen species that kill pathogens. Studies have shown that the unique mechanism of action of MPO does not induce resistance. The enzymes work by binding preferentially to pathogens, affecting multiple targets in the microbial cells of bacteria, fungi, and viruses while minimizing collateral damage to normal flora and host cells.

Antimicrobial activity

MPO and EPO have been shown in in vitro studies to have rapid cidal activity effective against a wide variety of antimicrobial-susceptible and antimicrobial-resistant pathogens, including:

Bacteria
(Aerobic and anaerobic gram-negative and gram-positive) Staphylococcus aureus, Pseudomonas aeruginosa, Escherichia coli, Streptococcus pyogenes, Streptococcus agalactiae, viridans streptococci, Enterobacter aerogenes, Enterobacter cloacae, Lactobacillus acidophilus, Propionibacterium acnes, Bacillus cereus, Clostridium sporogenes, Gardnerella vaginalis, Salmonella choleraesuis, Mycobacterium bovis, Mycobacterium terrae, Mycobacterium smegmatis, Chlamydia trachomatis, Chlamydia psittaci.

Molds and Yeasts
Aspergillus fumigatus, Aspergillus flavus, Trichophyton rubrum, Fusarium moniliforme, Candida albicans, Candida parapsilosis, Cryptococcus neoformans.

Viruses
Rhinovirus, HIV, bovine papillomavirus, herpes simplex virus.

A review of the scientific literature on haloperoxidase supports the broad microbicidal activity of MPO and EPO.