Work

Periplasmic Binding Protein YiuA Enables Yersinia pestis to Scavenge Fe(III)-Catechol Siderophores

Year: 2025

Type: article

Abstract: Yersinia pestis, the pathogen causing plague, requires iron to grow. Y. pestis employs several uptake pathways for iron, including the siderophore yersiniabactin, as well as hemin and inorganic iron. The Y. pestis iron assimilation repertoire further harbors the uncharacterized YiuRABC pathway, presumed to transport an unidentified Fe(III)-siderophore(s). Through intrinsic fluorescence quenching of the periplasmic binding protein YiuA, we discovered that YiuA displays high affinity toward Fe(III) complexes of the hydrolysis products of enterobactin, Fe(III)-[di(DHB- L Ser)] and Fe(III)-[DHB- L Ser] 2, with K d values of 27.6 ± 4.2 nM and 28.2 ± 6.9 nM, respectively, as well as the bis-catechol siderophore butanochelin, with K d 0.76 ± 0.17 nM. By comparison, YiuA has a much weaker affinity for intact Fe(III)-enterobactin, K d 444.7 ± 20.6 nM. Electronic circular dichroism spectroscopy reveals YiuA has a strong preference for binding Λ configured Fe(III)-siderophores, which can be achieved with the Fe(III) bis-catechol complexes but not Fe(III)-enterobactin.

Source: ACS Infectious Diseases

DOI: 10.1021/acsinfecdis.5c00524

Authors: Emil Thomsen, Parker Stow, Daniel Roth, Alison Butler

Institution: University of California, Santa Barbara

Language: English

Topic: Yersinia bacterium, plague, ectoparasites research

Subfield: Genetics

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funder: Division of Chemistry

Award: G8284193264