Open AccessAnalysis of outer membrane permeability of Pseudomonas aeruginosa and bactericidal activity of endolysins KZ144 and EL188 under high hydrostatic pressure
Author(s) -
Briers Yves,
Cornelissen Anneleen,
Aertsen Abram,
Hertveldt Kirsten,
Michiels Chris W.,
Volckaert Guido,
Lavigne Rob
Publication year - 2008
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2007.01051.x
Subject(s) - peptidoglycan , hydrostatic pressure , bacterial outer membrane , pseudomonas aeruginosa , lysin , lysozyme , chemistry , membrane permeability , microbiology and biotechnology , biophysics , biochemistry , membrane , biology , escherichia coli , enzyme , bacteria , bacteriophage , gene , physics , genetics , thermodynamics
The parameters influencing outer membrane permeability of Pseudomonas aeruginosa PAO1 under high hydrostatic pressure were quantified and optimized, using fusion between a specific A1γ peptidoglycan‐binding domain and green fluorescent protein (PBD–GFP). Based on the obtained data, optimal conditions were defined to assess the synergistic bactericidal action between high hydrostatic pressure and peptidoglycan hydrolysis by bacteriophage‐encoded endolysins KZ144 and EL188. Under high hydrostatic pressure, both endolysins show similar inactivation of P. aeruginosa as the commonly used hen egg white lysozyme or slightly higher inactivation in the case of EL188 at 150 and 200 MPa. The partial contribution of pressure to the bacterial inactivation increases with higher pressure, while the partial contribution of the enzymes is maximal at the onset pressure of outer membrane permeabilization for the PBD–GFP protein (175 MPa). This study's results demonstrate the usefulness of this approach to determine optimal synergy for hurdle technology applications.