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Identification of Functional LsrB-Like Autoinducer-2 Receptors

2009Journal article Open access
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dc.contributor.authorPereira, C. S.
dc.contributor.authorde Regt, A. K.
dc.contributor.authorBrito, P. H.
dc.contributor.authorMiller, S. T.
dc.contributor.authorXavier, K. B.
dc.date.accessioned2020-04-07T09:25:28Z
dc.date.available2020-04-07T09:25:28Z
dc.date.issued2009
dc.description.abstractAlthough a variety of bacterial species have been reported to use the interspecies communication signal autoinducer-2 (AI-2) to regulate multiple behaviors, the molecular mechanisms of AI-2 recognition and signal transduction remain poorly understood. To date, two types of AI-2 receptors have been identified: LuxP, present in Vibrio spp., and LsrB, first identified in Salmonella enterica serovar Typhimurium. In S. Typhimurium, LsrB is the ligand binding protein of a transport system that enables the internalization of AI-2. Here, using both sequence analysis and structure prediction, we establish a set of criteria for identifying functional AI-2 receptors. We test our predictions experimentally, assaying key species for their abilities to import AI-2 in vivo, and test their LsrB orthologs for AI-2 binding in vitro. Using these experimental approaches, we were able to identify AI-2 receptors in organisms belonging to phylogenetically distinct families such as the Enterobacteriaceae, Rhizobiaceae, and Bacillaceae. Phylogenetic analysis of LsrB orthologs indicates that this pattern could result from one single origin of the functional LsrB gene in a gammaproteobacterium, suggesting possible posterior independent events of lateral gene transfer to the Alphaproteobacteria and Firmicutes. Finally, we used mutagenesis to show that two AI-2-interacting residues are essential for the AI-2 binding ability. These two residues are conserved in the binding sites of all the functional AI-2 binding proteins but not in the non-AI-2-binding orthologs. Together, these results strongly support our ability to identify functional LsrB-type AI-2 receptors, an important step in investigations of this interspecies signal.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.doi10.1128/JB.00976-09pt_PT
dc.identifier.urihttp://hdl.handle.net/10400.7/952
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherAmerican Society for Microbiologypt_PT
dc.relationFCTpt_PT
dc.relation.publisherversionhttps://jb.asm.org/content/191/22/6975.longpt_PT
dc.subjectAgrobacterium tumefacienspt_PT
dc.subjectBacillaceaept_PT
dc.subjectBacterial Proteinspt_PT
dc.subjectBinding Sitespt_PT
dc.subjectEnterobacteriaceaept_PT
dc.subjectEscherichia colipt_PT
dc.subjectGenome, Bacterialpt_PT
dc.subjectPhylogenypt_PT
dc.subjectProtein Bindingpt_PT
dc.subjectReceptors, Cell Surfacept_PT
dc.subjectRhizobiaceaept_PT
dc.subjectRhizobium leguminosarumpt_PT
dc.subjectSalmonella typhimuriumpt_PT
dc.subjectStructure-Activity Relationshippt_PT
dc.titleIdentification of Functional LsrB-Like Autoinducer-2 Receptorspt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage6987pt_PT
oaire.citation.issue22pt_PT
oaire.citation.startPage6975pt_PT
oaire.citation.titleJournal of Bacteriologypt_PT
oaire.citation.volume191pt_PT
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT

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