{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sychantha D"],"funding":["Gouvernement du Canada | Canadian Institutes of Health Research","Gouvernement du Canada | Canadian Institutes of Health Research (Instituts de Recherche en Santé du Canada)"],"pagination":["4036"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11091072"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["Microbial Ni<sup>2+</sup> homeostasis underpins the virulence of several clinical pathogens. Ni<sup>2+</sup> 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 Zn<sup>2+</sup>, Ni<sup>2+</sup>, and Co<sup>2+</sup>. Here, we show that this specificity allows AMA to block the uptake of Ni<sup>2+</sup> and attenuate bacterial Ni-dependent enzymes, offering a potential strategy for reducing virulence. Bacterial exposure to AMA perturbs H<sub>2</sub> metabolism, ureolysis, struvite crystallization, and biofilm formation and shows efficac"],"journal":["Nature communications"],"pubmed_title":["Targeting bacterial nickel transport with aspergillomarasmine A suppresses virulence-associated Ni-dependent enzymes."],"pmcid":["PMC11091072"],"funding_grant_id":["FRN-I48463"],"pubmed_authors":["Prehna G","Sychantha D","Chen X","Koteva K","Wright GD"],"additional_accession":[]},"is_claimable":false,"name":"Targeting bacterial nickel transport with aspergillomarasmine A suppresses virulence-associated Ni-dependent enzymes.","description":"Microbial Ni<sup>2+</sup> homeostasis underpins the virulence of several clinical pathogens. Ni<sup>2+</sup> 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 Zn<sup>2+</sup>, Ni<sup>2+</sup>, and Co<sup>2+</sup>. Here, we show that this specificity allows AMA to block the uptake of Ni<sup>2+</sup> and attenuate bacterial Ni-dependent enzymes, offering a potential strategy for reducing virulence. Bacterial exposure to AMA perturbs H<sub>2</sub> metabolism, ureolysis, struvite crystallization, and biofilm formation and shows efficac","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-04-08T19:49:16.784Z","creation":"2026-04-08T14:31:16.17Z"},"accession":"S-EPMC11091072","cross_references":{"pubmed":["38740750"],"doi":["10.1038/s41467-024-48232-1"]}}