Targeting bacterial nickel transport with aspergillomarasmine A suppresses virulence-associated Ni-dependent enzymes.

ABSTRACT: Microbial Ni²⁺ homeostasis underpins the virulence of several clinical pathogens. Ni²⁺ is an essential cofactor in urease and [NiFe]-hydrogenases involved in colonization and persistence. Many microbes produce metallophores to sequester metals necessary for their metabolism and starve competing neighboring organisms. The fungal metallophore aspergillomarasmine A (AMA) shows narrow specificity for Zn²⁺, Ni²⁺, and Co²⁺. Here, we show that this specificity allows AMA to block the uptake of Ni²⁺ and attenuate bacterial Ni-dependent enzymes, offering a potential strategy for reducing virulence. Bacterial exposure to AMA perturbs H₂ metabolism, ureolysis, struvite crystallization, and biofilm formation and shows efficac

SUBMITTER: Sychantha D 

PROVIDER: S-EPMC11091072 | biostudies-literature | 2024 May

REPOSITORIES: biostudies-literature