A moonlighting serpin of Tannerella forsythia compromises the bactericidal activity of neutrophils
Serine protease inhibitors (serpins) are extremely rare in prokaryotes, and their role in immune evasion remains unclear. We identified a bifunctional TLR2-binding serpin (miropin) produced by Tannerella forsythia that broadly suppresses neutrophil antimicrobial capacity. Miropin binding to TLR2 primed neutrophils, enhancing phagocytic capacity yet, counterintuitively, promoting bacterial…
A serpin called miropin, produced by the bacterium Tannerella forsythia, has been discovered to compromise the bactericidal activity of neutrophils in an unexpected way. Despite its ability to inhibit neutrophil serine proteases (NSPs), miropin also binds and inhibits myeloperoxidase (MPO), blocking the oxidative burst. This dual mechanism allows miropin to suppress the overall antimicrobial capacity of neutrophils, enabling the bacterium to survive within the subgingival niche where it is frequently exposed to activated neutrophils.
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