Structural basis of iron piracy by human gut <i>Bacteroides</i>

upregulates an iron piracy system, XusABC, which steals iron-bound siderophores from the invading pathogens. Here, we investigated the molecular details of xenosiderophore uptake across the outer membrane by the XusAB complex. Our crystal and cryogenic electron microscopy structures explain how the XusB lipoprotein recognizes iron-bound xenosiderophores and passes them on to the XusA TonB-dependent transporter. Moreover, we show that Xus homologues can transport a variety of siderophores with different iron-chelating functional groups.

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Publication Details

Journal
Proceedings of the National Academy of Sciences
Published
2026-05-01
DOI
https://doi.org/10.1073/pnas.2528036123
Primary Topic
Bacterial Genetics and Biotechnology
Type
article
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article

Structural basis of iron piracy by human gut Bacteroides

Augustinas Silale, Arnaud Baslé, Elizabeth M. Nolan, Yung Li Soo et al.
Proceedings of the National Academy of Sciences
Bacterial Genetics and Biotechnology
article

Structural basis of iron piracy by human gut Bacteroides

Augustinas Silale, Arnaud Baslé, Elizabeth M. Nolan, Yung Li Soo, Hannah Mark, Rachel N Motz, Bert van den Berg
article en

Abstract

upregulates an iron piracy system, XusABC, which steals iron-bound siderophores from the invading pathogens. Here, we investigated the molecular details of xenosiderophore uptake across the outer membrane by the XusAB complex. Our crystal and cryogenic electron microscopy structures explain how the XusB lipoprotein recognizes iron-bound xenosiderophores and passes them on to the XusA TonB-dependent transporter. Moreover, we show that Xus homologues can transport a variety of siderophores with different iron-chelating functional groups.

Proceedings of the National Academy of SciencesVol. 123(18)
Massachusetts Institute of Technology (US), Newcastle University (GB)
Life below water
Openalex Percentile: Top 13%
Bacterial Genetics and Biotechnology
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