Publication
Identification of novel autoinducer-2 receptors in Clostridia reveals plasticity in the binding site of the LsrB receptor family
| dc.contributor.author | Torcato, Inês M. | |
| dc.contributor.author | Kasal, Meghann R. | |
| dc.contributor.author | Brito, Patrícia H. | |
| dc.contributor.author | Miller, Stephen T. | |
| dc.contributor.author | Xavier, Karina B. | |
| dc.date.accessioned | 2020-03-16T15:55:51Z | |
| dc.date.available | 2020-03-16T15:55:51Z | |
| dc.date.issued | 2019-03-22 | |
| dc.description.abstract | Autoinducer-2 (AI-2) is unique among quorum-sensing signaling molecules, as it is produced and recognized by a wide variety of bacteria and thus facilitates interspecies communication. To date, two classes of AI-2 receptors have been identified: the LuxP-type, present in the Vibrionales, and the LsrB-type, found in a number of phylogenetically distinct bacterial families. Recently, AI-2 was shown to affect the colonization levels of a variety of bacteria in the microbiome of the mouse gut, including members of the genus Clostridium, but no AI-2 receptor had been identified in this genus. Here, we identify a noncanonical, functional LsrB-type receptor in Clostridium saccharobutylicum. This novel LsrB-like receptor is the first one reported with variations in the binding-site amino acid residues that interact with AI-2. The crystal structure of the C. saccharobutylicum receptor determined at 1.35 Å resolution revealed that it binds the same form of AI-2 as the other known LsrB-type receptors, and isothermal titration calorimetry (ITC) assays showed that binding of AI-2 occurs at a submicromolar concentration. Using phylogenetic analysis, we inferred that the newly identified noncanonical LsrB receptor shares a common ancestor with known LsrB receptors and that noncanonical receptors are present in bacteria from different phyla. This led us to identify putative AI-2 receptors in bacterial species in which no receptors were known, as in bacteria belonging to the Spirochaetes and Actinobacteria phyla. Thus, this work represents a significant step toward understanding how AI-2-mediated quorum sensing influences bacterial interactions in complex biological niches. | pt_PT |
| dc.description.version | info:eu-repo/semantics/publishedVersion | pt_PT |
| dc.identifier.doi | 10.1074/jbc.RA118.006938 | pt_PT |
| dc.identifier.uri | http://hdl.handle.net/10400.7/939 | |
| dc.language.iso | eng | pt_PT |
| dc.peerreviewed | yes | pt_PT |
| dc.publisher | American Society for Biochemistry and Molecular Biology | pt_PT |
| dc.relation | FCT | pt_PT |
| dc.relation.publisherversion | https://www.jbc.org/content/294/12/4450.long | pt_PT |
| dc.subject | Amino Acid Substitution | pt_PT |
| dc.subject | Bacterial Proteins | pt_PT |
| dc.subject | Binding Sites | pt_PT |
| dc.subject | Calorimetry | pt_PT |
| dc.subject | Clostridium | pt_PT |
| dc.subject | Crystallography, X-Ray | pt_PT |
| dc.subject | Endocytosis | pt_PT |
| dc.subject | Homoserine | pt_PT |
| dc.subject | Lactones | pt_PT |
| dc.subject | Membrane Proteins | pt_PT |
| dc.subject | Microbiota | pt_PT |
| dc.subject | Phylogeny | pt_PT |
| dc.subject | Protein Binding | pt_PT |
| dc.subject | Protein Conformation | pt_PT |
| dc.subject | Quorum Sensing | pt_PT |
| dc.subject | Signal Transduction | pt_PT |
| dc.title | Identification of novel autoinducer-2 receptors in Clostridia reveals plasticity in the binding site of the LsrB receptor family | pt_PT |
| dc.type | journal article | |
| dspace.entity.type | Publication | |
| oaire.citation.endPage | 4463 | pt_PT |
| oaire.citation.issue | 12 | pt_PT |
| oaire.citation.startPage | 4450 | pt_PT |
| oaire.citation.title | Journal of Biological Chemistry | pt_PT |
| oaire.citation.volume | 294 | pt_PT |
| rcaap.rights | openAccess | pt_PT |
| rcaap.type | article | pt_PT |