Myeloperoxidase (MPO) and eosinophil peroxidase (EPO) provide the basis
for safe, broad-spectrum microbicidal agents against serious and resistant
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.
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:
(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.
Rhinovirus, HIV, bovine papillomavirus, herpes simplex virus.
A review of the scientific literature
on haloperoxidase supports the broad microbicidal activity of MPO and