Abstract
The innate immune system antibacterial protein Siderocalin (Scn) binds ferric carboxymycobactin (CMB) and also several catecholate siderophores. Although the recognition of catecholates by Scn has been thoroughly investigated, the binding interactions of Scn with the full spectrum of CMB isoforms have not been studied. Here we show that Scn uses different binding modes for the limited subset of bound CMB isoforms, resulting in a range of binding affinities that are much weaker than other siderophore targets of Scn. Understanding the binding interaction between Scn and CMBs provides clues for the influence of Scn on mycobacterial iron acquisition.
Publication types
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Letter
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Research Support, N.I.H., Extramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Acute-Phase Proteins / physiology*
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Carrier Proteins / physiology*
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Humans
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Immunity, Innate
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Iron / metabolism*
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Iron Chelating Agents / metabolism
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Iron Chelating Agents / pharmacology
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Lipocalin-2
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Lipocalins / physiology*
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Models, Molecular
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Molecular Conformation
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Mycobacterium tuberculosis / drug effects
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Mycobacterium tuberculosis / metabolism*
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Oxazoles / chemistry
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Oxazoles / metabolism*
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Proto-Oncogene Proteins / physiology*
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Static Electricity
Substances
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Acute-Phase Proteins
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Carrier Proteins
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Iron Chelating Agents
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LCN2 protein, human
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Lipocalin-2
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Lipocalins
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Oxazoles
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Proto-Oncogene Proteins
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mycobactins
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Iron