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Title

Proteomic and functional analyses reveal a unique lifestyle for acinetobacter baumannii biofilms and a key role for histidine metabolism

AuthorsCabral, María P.; Soares, Nelson C.; Aranda, Jesús; Parreira, José R.; Rumbo, Carlos; Poza, Margarita; Valle Turrillas, Jaione ; Calamia, Valentina; Lasa, Íñigo ; Bou, Germán
Issue Date2011
PublisherAmerican Chemical Society
CitationJournal of Proteome Research 10(8): 3399-3417 (2011)
AbstractBiofilm formation is one of the main causes for the persistence of Acinetobacter baumannii, a pathogen associated with severe infections and outbreaks in hospitals. Here, we performed comparative proteomic analyses (2D-DIGE and MALDI-TOF/TOF and iTRAQ/SCX-LC-MS/MS) of cells at three different conditions: exponential, late stationary phase, and biofilms. These results were compared with alterations in the proteome resulting from exposure to a biofilm inhibitory compound (salicylate). Using this multiple-approach strategy, proteomic patterns showed a unique lifestyle for A. baumannii biofilms and novel associated proteins. Several cell surface proteins (such as CarO, OmpA, OprD-like, DcaP-like, PstS, LysM, and Omp33), as well as those involved in histidine metabolism (like Urocanase), were found to be implicated in biofilm formation, this being confirmed by gene disruption. Although l-His uptake triggered biofilms efficiently in wild-type A. baumannii, no effect was observed in Urocanase and OmpA mutants, while a slight increase was observed in a CarO deficient strain. We conclude that Urocanase plays a crucial role in histidine metabolism leading to biofilm formation and that OmpA and CarO can act as channels for l-His uptake. Finally, we propose a model in which novel proteins are suggested for the first time as targets for preventing the formation of A. baumannii biofilms. © 2011 American Chemical Society.
URIhttp://hdl.handle.net/10261/50700
DOI10.1021/pr101299j
Identifiersdoi: 10.1021/pr101299j
issn: 1535-3893
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