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.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Rodas PI,Álamos-Musre AS,Álvarez FP,Escobar A,Tapia CV,Osorio E,Otero C,Calderón IL,Fuentes JA,Gil F,Paredes-Sabja D,Christodoulides Mdoi
10.1093/femsle/fnw181subject
Has Abstractpub_date
2016-09-01 00:00:00issue
17eissn
0378-1097issn
1574-6968pii
fnw181journal_volume
363pub_type
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