INVESTIGADORES
CHALON Miriam Carolina
congresos y reuniones científicas
Título:
DEVELOPMENT OF A SUICIDE PROBE BASED ON PEDIOCIN PA?1 THAT IS ACTIVE AGAINST Escherichia coli
Autor/es:
RIOS COLOMBO, N.S.; CHALON M.C.; BELLOMIO, A; MINAHK, C.J
Lugar:
Mar del Plata
Reunión:
Congreso; LI Reunión Anual de la Sociedad Argentina de Investigación Bioquímica y Biología Molecular (SAIB); 2015
Institución organizadora:
SAIB
Resumen:
Pediocin PA-1 is a subclass IIa bacteriocin produced by Pediococcus acidilactici. This group of peptides acts on thecell membrane of Gram (+) bacteria by forming pores. Apparently, these peptides bind to a membrane specificreceptor. The theories on pore formation mechanism by bacteriocins suggest that they would induce conformationalchanges on the receptor to form a channel that remains open or, they would just use the receptor as an anchor andthen form the pore. In both cases, pore formation causes leakage of ions, dissipation of proton motive force andrelease of essential metabolites. In order to study the mechanism by which Pediocin PA-1 induces the loss ofmembrane integrity, we led the bacteriocin to the cell membrane of E. coli, by a transcriptional fusion of the peptidewith EtpM, a protein of the type II secretion system from E. coli O157: H7. In this work we constructed the fusionetpM-pedA under the tight control of PBAD promoter (repressed by glucose and induced by arabinose). In addition wecarried out the co-expression of EtpM-PedA with the Pediocin PA-1 immunity protein. The results show thatPediocin PA-1 is capable of acting on Gram-negative bacteria when it is anchored in the plasmatic membrane,independently of its specific receptor. This suicidal probe will allow a deeper study of the mechanism of action ofbacteriocins and its immunity proteins, using an in vivo system