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

Resultado de la investigación: Contribución a una revistaArtículorevisión exhaustiva

3 Citas (Scopus)

Resumen

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.

Idioma originalInglés
Número de artículofnw181
PublicaciónFEMS Microbiology Letters
Volumen363
N.º17
DOI
EstadoPublicada - 1 sep 2016

Áreas temáticas de ASJC Scopus

  • Microbiología
  • Biología molecular
  • Genética

Huella

Profundice en los temas de investigación de 'The NarE protein of neisseria gonorrhoeae catalyzes ADP-ribosylation of several ADP-ribose acceptors despite an N-terminal deletion'. En conjunto forman una huella única.

Citar esto