INVESTIGADORES
DUPUY Fernando Gabriel
congresos y reuniones científicas
Título:
Suicide probes and Laurdan as tools to assess in vivo bacteriocin-membrane interactions.
Autor/es:
RÍOS COLOMBO, N.S.; CHALÓN, M.C.; DUPUY, FERNANDO G.; BELLOMIO, A.
Lugar:
San Luis
Reunión:
Congreso; XLVIII Reunión Anual de la Sociedad Argentina de Biofísica; 2019
Institución organizadora:
Sociedad Argentina de Biofísica
Resumen:
The study of alternative antimicrobials, like bacteriocins, has become relevant in the last years because of the increasing resistance to common antibiotics. Class II bacteriocins are unmodified membrane-active peptides that act over a narrow spectrum of bacterial targets. They bind a specific receptor on the membrane that would participate in the formation of a pore, leading to membrane permeabilization and cell death. To reveal whether or not the pore structure involves the specific receptor, we designed chimeric peptides (also called SUICIDE PROBES) fusing the bitopic membrane protein EtpM with different class II bacteriocins: enterocin CRL35, pediocin PA-1 and microcin V. The EtpM-bacteriocins were heterologously expressed in E. coli and E. coli sdaCrespectively. We chose these expression hosts because they lack their specific receptor for enterocin and pediocin. In addition, E. coli sdaC mutant was employed as a receptor-free host for MccV. So far, there has been several studies on bacteriocin-membrane interactions, mainly using model membranes. Although in vitro approaches are very useful to understand bacteriocins mechanism of action, these models demand to simplify an extremely complex and dynamic system such as the biological membrane. In this work we study the effect of three bacteriocins in membrane fluidity using Laurdan and fluorescent spectroscopy, with real bacterial membranes, as a tool to complement studies in model membranes.