Rodas, Paula I.Álamos-Musre, A. SaidÁlvarez, Francisca P.Escobar, AlejandroTapia, Cecilia V.Osorio, EduardoOtero, CarolinaCalderón, Iván L.Fuentes, Juan A.Gil, FernandoParedes-Sabja, DanielChristodoulides, Myron2023-09-272023-09-272016-09FEMS Microbiology Letters. Volume 363, Issue 17. 1 September 2016. Article number fnw1810378-1097https://repositorio.unab.cl/xmlui/handle/ria/53342Indexación: Scopus.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.enNarENeisseria GonorrhoeaeADP-RibosyltransferaseArtículo10.1093/femsle/fnw181