The NarE protein of neisseria gonorrhoeae catalyzes ADP-ribosylation of several ADP-ribose acceptors despite an N-terminal deletion
dc.contributor.author | Rodas, Paula I. | |
dc.contributor.author | Álamos-Musre, A. Said | |
dc.contributor.author | Álvarez, Francisca P. | |
dc.contributor.author | Escobar, Alejandro | |
dc.contributor.author | Tapia, Cecilia V. | |
dc.contributor.author | Osorio, Eduardo | |
dc.contributor.author | Otero, Carolina | |
dc.contributor.author | Calderón, Iván L. | |
dc.contributor.author | Fuentes, Juan A. | |
dc.contributor.author | Gil, Fernando | |
dc.contributor.author | Paredes-Sabja, Daniel | |
dc.contributor.author | Christodoulides, Myron | |
dc.date.accessioned | 2023-09-27T15:31:39Z | |
dc.date.available | 2023-09-27T15:31:39Z | |
dc.date.issued | 2016-09 | |
dc.description | Indexación: Scopus. | es |
dc.description.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. | es |
dc.description.uri | https://academic-oup-com.recursosbiblioteca.unab.cl/femsle/article/363/17/fnw181/2197729 | |
dc.identifier.citation | FEMS Microbiology Letters. Volume 363, Issue 17. 1 September 2016. Article number fnw181 | es |
dc.identifier.doi | 10.1093/femsle/fnw181 | |
dc.identifier.issn | 0378-1097 | |
dc.identifier.uri | https://repositorio.unab.cl/xmlui/handle/ria/53342 | |
dc.language.iso | en | es |
dc.publisher | Oxford University Press | es |
dc.subject | NarE | es |
dc.subject | Neisseria Gonorrhoeae | es |
dc.subject | ADP-Ribosyltransferase | es |
dc.title | The NarE protein of neisseria gonorrhoeae catalyzes ADP-ribosylation of several ADP-ribose acceptors despite an N-terminal deletion | es |
dc.type | Artículo | es |
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