10.1021/cb200331g.s001
Trisha M. Hoette
Trisha M.
Hoette
Matthew C. Clifton
Matthew C.
Clifton
Anna M. Zawadzka
Anna M.
Zawadzka
Meg A. Holmes
Meg A.
Holmes
Roland K. Strong
Roland K.
Strong
Kenneth N. Raymond
Kenneth N.
Raymond
Immune Interference in <i>Mycobacterium tuberculosis</i> Intracellular Iron Acquisition through Siderocalin Recognition of Carboxymycobactins
American Chemical Society
2016
binding
mycobacterial iron acquisition
Scn
CMB isoforms
Mycobacterium tuberculosis Intracellular Iron Acquisition
2016-02-22 11:17:52
Journal contribution
https://acs.figshare.com/articles/journal_contribution/Immune_Interference_in_i_Mycobacterium_tuberculosis_i_Intracellular_Iron_Acquisition_through_Siderocalin_Recognition_of_Carboxymycobactins/2570389
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.