How Pathogens Evolve New Metal Appetites
A new study reveals the molecular mechanism by which pathogenic bacteria can evolve to switch their preferred metal cofactor, a key adaptation for survival within a host. Researchers focused on the superoxide dismutase (SodFM) enzyme family, which can use either iron or manganese. By analyzing the oxidation states of these metals across diverse enzymes, they discovered a direct link between an enzyme’s resting metal oxidation state and its catalytic metal preference. Crucially, mutagenesis experiments showed that second-sphere residues, which form the cofactor’s secondary coordination sphere, tune this redox property, thereby controlling whether the enzyme is optimized for iron or manganese. This redox modulation provides a clear evolutionary pathway for metalloenzymes to adapt to changing environmental metal availability.
Why it might matter to you: This work provides a fundamental understanding of how microbial pathogens like bacteria evolve resistance to host nutritional immunity, which often restricts metal availability. For professionals in antimicrobial research and microbial pathogenesis, it identifies a specific, tunable mechanism—redox tuning via the secondary coordination sphere—that could inform new strategies to disrupt essential metalloenzyme function. It directly connects core concepts in microbial genetics and host–microbe interactions to a tangible evolutionary adaptation with implications for combating antimicrobial resistance.
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