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. 2013 Aug 20;4(4):e00459-13. doi: 10.1128/mBio.00459-13

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Copyright © 2013 Traxler et al.

This is an open-access article distributed under the terms of the Creative Commons Attribution-Noncommercial-ShareAlike 3.0 Unported license, which permits unrestricted noncommercial use, distribution, and reproduction in any medium, provided the original author and source are credited.

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FIG 5 — Patterns of acyl-desferrioxamine production in interspecies interactions. (A) Heat map of acyl-desferrioxamine production. Analysis parameters are identical to those in Fig. 3C. (B) Subnetworks 1 and 2 contain the majority of acyl-desferrioxamines verified by MS2 fragmentation. Fine-scale analysis of subnetwork 1 is shown, illustrating differential acyl-desferrioxamine production in various interactions over time. Note the proximity of subnetwork 1 to desferrioxamine B (DFO B). Subnetworks 3 and 4 contain larger versions of DFOs and sodium adducts, respectively (see Fig. S3 at http://gasp.med.harvard.edu/journals/traxler_2013_SI_nanodesi.pdf). (C) Desferrioxamines are observable using IMS at day 5. m/z 561 and 601 correspond to desferrioxamines B and E, respectively. m/z 701 to 785 are representative acyl-desferrioxamines. Note the production of acyl-desferrioxamines by S. coelicolor in interactions where initiator strains do not make desferrioxamines B and/or E. Each IMS signal is scaled as a single color heat map; brighter color indicates higher signal intensity, and darker indicates lower signal intensity. (D) Acyl-desferrioxamines diffuse away from S. coelicolor colonies in three dimensions. The outermost to innermost layers (isosurfaces) correspond to 0.8, 0.88, and 0.95% ion intensity.