Synopsis

Source of validity: Scientific
Rating (out of 5): 2

Lactoperoxidase is an enzyme found in milk and other body fluids that plays a role in the innate immune system by catalyzing the oxidation of thiocyanate ions in the presence of hydrogen peroxide to produce antimicrobial substances. The interest in lactoperoxidase as a supportive treatment for viral infections, including Herpes simplex virus (HSV), arises from its demonstrated antiviral properties in vitro.

Several laboratory studies have shown that the lactoperoxidase system can inactivate or inhibit replication of various viruses, including HSV-1 and HSV-2, through the generation of reactive oxygen species and hypothiocyanite, which can disrupt viral envelopes or interfere with viral proteins. For instance, some in vitro research (e.g., Nagasawa et al., 1996; Thomas et al., 1988) has shown that the lactoperoxidase system can suppress HSV infectivity in controlled environments.

However, direct clinical evidence supporting the use of lactoperoxidase for treating or preventing herpes infections in humans is limited. Most evidence comes from cell culture studies rather than clinical trials. There is interest in lactoperoxidase-containing oral care products and topical formulations for reducing HSV outbreaks, but robust randomized controlled trials are lacking.

In summary, while there is scientific rationale and in vitro evidence for the antiviral effects of lactoperoxidase against herpes viruses, the current level of evidence for its clinical use in treating or supporting herpes is weak (hence the rating of 2/5), and more human studies are needed to confirm efficacy and safety.

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