425979 Heterologous Biosynthesis and Diverse Applications for the Nonribosomal Peptide-Polyketide Siderophore Yersiniabactin (Rapid Fire)

Wednesday, November 11, 2015
Exhibit Hall 1 (Salt Palace Convention Center)
Mahmoud Kamal Ahmadi, Chemical and Biological Engineering, Satate University of New York at Buffalo, Buffalo, NY and Blaine A. Pfeifer, Department of Chemical and Biological Engineering, SUNY-Buffalo, Buffalo, NY

Yersiniabactin (Ybt) is a mixed nonribosomal peptide-polyketide natural product natively produced by the pathogen Yersinia pestis.  The compound enables iron scavenging capabilities upon host infection and is biosynthesized by a nonribosomal peptide synthetase featuring a polyketide synthase module.  This pathway has been engineered for expression and biosynthesis using Escherichia coli as a heterologous host.  In the current work, the biosynthetic process for Ybt formation has been improved through the incorporation of a dedicated step to eliminate the need for exogenous salicylate provision.  Upon doing so, the compound was tested in parallel applications that highlight the metal chelating nature of the compound.  In the first application, Ybt was assessed as a rust remover, demonstrating a capacity of ~40% compared to a commercial removal agent and ~20% relative to total removal capacity.  The second application tested Ybt in removing copper from a variety of non-biological and biological solution mixtures.  Success across a variety of media indicates potential utility in broad settings that include environmental and biomedical contexts.

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