Your browser doesn't support javascript.
loading
A Family of T6SS Antibacterial Effectors Related to l,d-Transpeptidases Targets the Peptidoglycan.
Sibinelli-Sousa, Stephanie; Hespanhol, Julia T; Nicastro, Gianlucca G; Matsuyama, Bruno Y; Mesnage, Stephane; Patel, Ankur; de Souza, Robson F; Guzzo, Cristiane R; Bayer-Santos, Ethel.
Afiliación
  • Sibinelli-Sousa S; Departamento de Microbiologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo 05508-900, Brazil.
  • Hespanhol JT; Departamento de Microbiologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo 05508-900, Brazil.
  • Nicastro GG; Departamento de Microbiologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo 05508-900, Brazil.
  • Matsuyama BY; Departamento de Bioquímica, Instituto de Química, Universidade de São Paulo, São Paulo 05508-000, Brazil.
  • Mesnage S; Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, UK.
  • Patel A; Department of Molecular Biology and Biotechnology, University of Sheffield, Sheffield S10 2TN, UK.
  • de Souza RF; Departamento de Microbiologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo 05508-900, Brazil.
  • Guzzo CR; Departamento de Microbiologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo 05508-900, Brazil.
  • Bayer-Santos E; Departamento de Microbiologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo 05508-900, Brazil. Electronic address: ebayersantos@usp.br.
Cell Rep ; 31(12): 107813, 2020 06 23.
Article en En | MEDLINE | ID: mdl-32579939
Type VI secretion systems (T6SSs) are nanomachines used by bacteria to inject toxic effectors into competitors. The identity and mechanism of many effectors remain unknown. We characterized a Salmonella T6SS antibacterial effector called Tlde1 that is toxic in target-cell periplasm and is neutralized by its cognate immunity protein (Tldi1). Microscopy analysis reveals that cells expressing Tlde1 stop dividing and lose cell envelope integrity. Bioinformatic analysis uncovers similarities between Tlde1 and the catalytic domain of l,d-transpeptidases. Point mutations on conserved catalytic residues abrogate toxicity. Biochemical assays reveal that Tlde1 displays both l,d-carboxypeptidase activity by cleaving peptidoglycan tetrapeptides between meso-diaminopimelic acid3 and d-alanine4 and l,d-transpeptidase exchange activity by replacing d-alanine4 by a non-canonical d-amino acid. Phylogenetic analysis shows that Tlde1 homologs constitute a family of T6SS-associated effectors broadly distributed among Proteobacteria. This work expands our current knowledge about bacterial effectors used in interbacterial competition and reveals a different mechanism of bacterial antagonism.
Asunto(s)
Palabras clave
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Peptidoglicano / Peptidil Transferasas / Sistemas de Secreción Tipo VI / Antibacterianos Idioma: En Revista: Cell Rep Año: 2020 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Peptidoglicano / Peptidil Transferasas / Sistemas de Secreción Tipo VI / Antibacterianos Idioma: En Revista: Cell Rep Año: 2020 Tipo del documento: Article País de afiliación: Brasil Pais de publicación: Estados Unidos