Although pseudomonads are not obligate pathogens, many species are capable of causing disease in a wide variety of hosts [3, 4]. As iron restriction is a key host defense mechanism, pyoverdine is frequently implicated as an important virulence factor [5, 6]. Pyoverdine is synthesized from amino acid precursors by non-ribosomal peptide synthetase enzymes

(NRPS) [7, 8]. It is pyoverdine that provides the fluorescent Pseudomonas species with their defining fluorescence and yellow-green pigmentation RG-7388 manufacturer under conditions of iron limitation [9]. These properties derive from an invariant dihydroxyquinoline chromophore, to which is attached an acyl moiety and a strain-specific peptide side chain [10]. More than 50 different pyoverdine structures have been described to date [11] and the variability of the peptide side chain of pyoverdines from different strains reflects rapid evolution of both the NRPS that synthesize this side chain and the outer membrane receptors that recognize ferric pyoverdine [12]. Analysis of the pyoverdine locus of different P. aeruginosa strains indicated that it is the most divergent region in

the core genome and that its evolution has been substantially shaped by horizontal gene transfer [12, 13]. The diversification of pyoverdine structures is particularly interesting when viewed in the context of NRPS manipulation experiments [[14–16]] – the wide variety of pyoverdine structures that has resulted from natural recombination of a limited pool of NRPS

modules provides clues as to how nature has overcome the barriers that frequently limit artificial recombination of selleck products NRPS enzymes [16, 17]. Moreover, the ability to detect pyoverdine production at nanomolar levels by UV-fluorescent screening [18] makes the pyoverdine synthetases potentially a very attractive model system to study NRPS recombination. However, in terms of providing ‘raw material’ for such work, the only biochemical analysis of a pyoverdine new NRPS to date focused on the L-threonine incorporating enzyme PvdD of P. aeruginosa PAO1 [19]. In the work described here we aimed to expand this focus to the NRPS enzymes of another fluorescent pseudomonad, Pseudomonas syringae pv. phaseolicola 1448a (P. syringae 1448a), which secretes an alternative form of pyoverdine to PAO1. During the course of this study, pyoverdine null mutants were generated, revealing that P. syringae 1448a (like P. syringae pathovars syringae B728a [20], syringae 22d/93 [21], and glycinea 1a/96 [21]) produces achromobactin as a secondary siderophore. In contrast to pyoverdine, achromobactin is synthesized by a mechanism that is entirely independent of NRPS enzymes [22]. NRPS-independent siderophores have been selleck inhibitor studied far less intensively than their NRPS-dependent counterparts, and their mechanisms of synthesis have only recently begun to be deciphered.