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Identification of novel autoinducer-2 receptors in Clostridia reveals plasticity in the binding site of the LsrB receptor family.
Torcato, Inês M; Kasal, Meghann R; Brito, Patrícia H; Miller, Stephen T; Xavier, Karina B.
Afiliação
  • Torcato IM; From the Instituto Gulbenkian de Ciência, Rua da Quinta Grande, 6, 2780-156 Oeiras, Portugal.
  • Kasal MR; the Instituto de Tecnologia Química e Biológica António Xavier, Universidade NOVA de Lisboa, Avenida da República, 2780-157 Oeiras, Portugal.
  • Brito PH; the Department of Chemistry and Biochemistry, Swarthmore College, Swarthmore, Pennsylvania 19081, and.
  • Miller ST; From the Instituto Gulbenkian de Ciência, Rua da Quinta Grande, 6, 2780-156 Oeiras, Portugal.
  • Xavier KB; the Chronic Disease Research Center (CEDOC), NOVA Medical School, Universidade NOVA de Lisboa, Rua Câmara Pestana, 6, 1150-082 Lisboa, Portugal.
J Biol Chem ; 294(12): 4450-4463, 2019 03 22.
Article em En | MEDLINE | ID: mdl-30696769
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.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Clostridium / Homosserina / Lactonas / Proteínas de Membrana Idioma: En Ano de publicação: 2019 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteínas de Bactérias / Clostridium / Homosserina / Lactonas / Proteínas de Membrana Idioma: En Ano de publicação: 2019 Tipo de documento: Article