The NarE protein of neisseria gonorrhoeae catalyzes ADP-ribosylation of several ADP-ribose acceptors despite an N-terminal deletion

Paula I. Rodas, A. Said Álamos-Musre, Francisca P. Álvarez1, Alejandro Escobar, Cecilia V. Tapia, Eduardo Osorio, Carolina Otero, Iván L. Calderón, Juan A. Fuentes, Fernando Gil, Daniel Paredes-Sabja, Myron Christodoulides

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

The ADP-ribosylating enzymes are encoded in many pathogenic bacteria in order to affect essential functions of the host. In this study, we show that Neisseria gonorrhoeae possess a locus that corresponds to the ADP-ribosyltransferase NarE, a previously characterized enzyme in N. meningitidis. The 291 bp coding sequence of gonococcal narE shares 100% identity with part of the coding sequence of the meningococcal narE gene due to a frameshift previously described, thus leading to a 49-amino-acid deletion at the N-terminus of gonococcal NarE protein. However, we found a promoter region and a GTG start codon, which allowed expression of the protein as demonstrated by RT-PCR and western blot analyses. Using a gonococcal NarE-6xHis fusion protein, we demonstrated that the gonococcal enzyme underwent auto-ADP-ribosylation but to a lower extent than meningococcal NarE. We also observed that gonoccocal NarE exhibited ADP-ribosyltransferase activity using agmatine and cell-free host proteins as ADP-ribose acceptors, but its activity was inhibited by human β-defensins. Taken together, our results showed that NarE of Neisseria gonorrhoeae is a functional enzyme that possesses key features of bacterial ADP-ribosylating enzymes.

Original languageEnglish
Article numberfnw181
JournalFEMS Microbiology Letters
Volume363
Issue number17
DOIs
Publication statusPublished - 1 Sep 2016

Keywords

  • ADP-ribosyltransferase
  • NarE
  • Neisseria gonorrhoeae

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics

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