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Masignani, Vega; Balducci, Enrico; Di Marcello, Federica; Savino, Silvana; Serruto, Davide; Veggi, Daniele; Bambini, Stefania; Scarselli, Maria; Aricò, Beatrice; Comanducci, Maurizio; Adu‐Bobie, Jeannette; Giuliani, Marzia M.; Rappuoli, Rino; Pizza, Mariagrazia

NarE: a novel ADP‐ribosyltransferase from Neisseria meningitidis

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  • Media type: E-Article
  • Title: NarE: a novel ADP‐ribosyltransferase from Neisseria meningitidis
  • Contributor: Masignani, Vega; Balducci, Enrico; Di Marcello, Federica; Savino, Silvana; Serruto, Davide; Veggi, Daniele; Bambini, Stefania; Scarselli, Maria; Aricò, Beatrice; Comanducci, Maurizio; Adu‐Bobie, Jeannette; Giuliani, Marzia M.; Rappuoli, Rino; Pizza, Mariagrazia
  • imprint: Wiley, 2003
  • Published in: Molecular Microbiology
  • Language: English
  • DOI: 10.1046/j.1365-2958.2003.03770.x
  • ISSN: 0950-382X; 1365-2958
  • Keywords: Molecular Biology ; Microbiology
  • Origination:
  • Footnote:
  • Description: <jats:title>Summary</jats:title><jats:p>Mono ADP‐ribosyltransferases (ADPRTs) are a class of functionally conserved enzymes present in prokaryotic and eukaryotic organisms. In bacteria, these enzymes often act as potent toxins and play an important role in pathogenesis. Here we report a profile‐based computational approach that, assisted by secondary structure predictions, has allowed the identification of a previously undiscovered ADP‐ribosyltransferase in <jats:italic>Neisseria meningitidis</jats:italic> (NarE). NarE shows structural homologies with <jats:italic>E. coli</jats:italic> heat‐labile enterotoxin (LT) and cholera toxin (CT) and possesses ADP‐ribosylating and NAD‐glycohydrolase activities. As in the case of LT and CT, NarE catalyses the transfer of the ADP‐ribose moiety to arginine residues. Despite the absence of a signal peptide, the protein is efficiently exported into the periplasm of <jats:italic>Neisseria</jats:italic>. The <jats:italic>narE</jats:italic> gene is present in 25 out of 43 strains analysed, is always present in ET‐5 and Lineage 3 but absent in ET‐37 and Cluster A4 hypervirulent lineages. When present, the gene is 100% conserved in sequence and is inserted upstream of and co‐transcribed with the lipoamide dehydrogenase E3 gene. Possible roles in the pathogenesis of <jats:italic>N. meningitidis</jats:italic> are discussed.</jats:p>
  • Access State: Open Access