INVESTIGADORES
SAAVEDRA Maria Lucila
artículos
Título:
Short peptides derived from the NH2-terminus of subclass IIa bacteriocin enterocin CRL35 show antimicrobial activity.
Autor/es:
EMILIANO SALVUCCI, LUCILA SAAVEDRA AND FERNANDO SESMA
Revista:
JOURNAL OF ANTIMICROBIAL CHEMOTHERAPY
Referencias:
Año: 2007 p. 1102 - 1108
ISSN:
0305-7453
Resumen:
Objectives: Subclass IIa bacteriocins are characterized by a hydrophilic N-terminal domain that
shares a YGNGVxCxxxxC consensus and a variable hydrophobic C-terminus. Enterocin CRL35 is a 43-
amino-acid heat stable peptide with antilisterial activity. Short synthetic peptides derived from the
N-terminal half of enterocin CRL35 and other subclass IIa bacteriocins were evaluated for antimicrobial
properties.
shares a YGNGVxCxxxxC consensus and a variable hydrophobic C-terminus. Enterocin CRL35 is a 43-
amino-acid heat stable peptide with antilisterial activity. Short synthetic peptides derived from the
N-terminal half of enterocin CRL35 and other subclass IIa bacteriocins were evaluated for antimicrobial
properties.
: Subclass IIa bacteriocins are characterized by a hydrophilic N-terminal domain that
shares a YGNGVxCxxxxC consensus and a variable hydrophobic C-terminus. Enterocin CRL35 is a 43-
amino-acid heat stable peptide with antilisterial activity. Short synthetic peptides derived from the
N-terminal half of enterocin CRL35 and other subclass IIa bacteriocins were evaluated for antimicrobial
properties.
Methods: In vitro activities of synthetic peptides were evaluated in complex, chemically defined and
minimal media. MIC assays were performed by the agar well-diffusion method. Fluorescence assays to
evaluate the dissipation of membrane potentials in intact cells were carried out. Timekill kinetics of
minimal media. MIC assays were performed by the agar well-diffusion method. Fluorescence assays to
evaluate the dissipation of membrane potentials in intact cells were carried out. Timekill kinetics of
: In vitro activities of synthetic peptides were evaluated in complex, chemically defined and
minimal media. MIC assays were performed by the agar well-diffusion method. Fluorescence assays to
evaluate the dissipation of membrane potentials in intact cells were carried out. Timekill kinetics of
Listeria innocua cells with the active peptide were performed.cells with the active peptide were performed.
Results and conclusions: A 15-mer peptide derived from enterocin CRL35 inhibited the growth of: A 15-mer peptide derived from enterocin CRL35 inhibited the growth of
L. innocua and Listeria monocytogenes in synthetic/minimal media and dissipated the membrane
potential of sensitive cells, with MICs of 10 and 50 mM, respectively. 15-mer derivatives from other
class IIa bacteriocins (mesentericin Y105, pediocin PA-1 and piscicolin 126) also showed antimicrobial
activities.
class IIa bacteriocins (mesentericin Y105, pediocin PA-1 and piscicolin 126) also showed antimicrobial
activities.
potential of sensitive cells, with MICs of 10 and 50 mM, respectively. 15-mer derivatives from other
class IIa bacteriocins (mesentericin Y105, pediocin PA-1 and piscicolin 126) also showed antimicrobial
activities.
class IIa bacteriocins (mesentericin Y105, pediocin PA-1 and piscicolin 126) also showed antimicrobial
activities.
. innocua and Listeria monocytogenes in synthetic/minimal media and dissipated the membrane
potential of sensitive cells, with MICs of 10 and 50 mM, respectively. 15-mer derivatives from other
class IIa bacteriocins (mesentericin Y105, pediocin PA-1 and piscicolin 126) also showed antimicrobial
activities.
class IIa bacteriocins (mesentericin Y105, pediocin PA-1 and piscicolin 126) also showed antimicrobial
activities.
mM, respectively. 15-mer derivatives from other
class IIa bacteriocins (mesentericin Y105, pediocin PA-1 and piscicolin 126) also showed antimicrobial
activities.