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Response of spheroplasts and chelator-permeabilized cells of Gram-negative bacteria to the action of the bacteriocins pediocin SJ-1 and nisin
Year:
1994
Authors :
Schved, Fernando
;
.
Volume :
21
Co-Authors:
Schved, F., Institute of Technology and Storage of Agricultural Products, Agricultural Research Organization, The Volcani Centre, Bet-Dagan, Israel
Henis, Y., Department of Plant Pathology and Microbiology, the Otto Warburg Centre for Biotechnology in Agriculture, The Hebrew University of Jerusalem, Rehovot, Israel
Juven, B.J., Institute of Technology and Storage of Agricultural Products, Agricultural Research Organization, The Volcani Centre, Bet-Dagan, Israel
Facilitators :
From page:
305
To page:
314
(
Total pages:
10
)
Abstract:
We have attempted to bypass the outer membrane (OM) barrier of Escherichia coli and Salmonella typhimurium with pediocin SJ-1 (as compared with nisin) using chelating agents as OM permeabilizers. EDTA, and to less extent EGTA, enabled nisin, but not pediocin SJ-1, to permeate the cell OM of E. coli, to have access to the cytoplasmic membrane and to cause subsequent permeability changes, indicated by an increase in ANS fluorescence intensity and a shift of its emission maximum. Such spectral changes did not occur when, prior to addition, EDTA was saturated with Ca2+ and Mg2+. ANS fluorescence data indicated that, in spite of the fact that pediocin SJ-1 did traverse the EDTA-permeabilized OM of E. coli, it did not cause perturbation of its cytoplasmic membrane and was, therefore, unable to cause cell death. Spheroplasts prepared from E. coli were lysed when treated with nisin but not with pediocin SJ-1. We suggest that the resistance of Gram-negative bacteria to pediocin SJ-1 is due not only to this material's inability to permeate the OM but also (in contrast to nisin) to its inability to interact with the cytoplasmic membrane. © 1994.
Note:
Related Files :
Animal
bacteriocin
Bacteriocins
cell membrane
Chickens
meat
nisin
unclassified drug
Show More
Related Content
More details
DOI :
10.1016/0168-1605(94)90060-4
Article number:
Affiliations:
Database:
Scopus
Publication Type:
article
;
.
Language:
English
Editors' remarks:
ID:
24102
Last updated date:
02/03/2022 17:27
Creation date:
17/04/2018 00:05
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Scientific Publication
Response of spheroplasts and chelator-permeabilized cells of Gram-negative bacteria to the action of the bacteriocins pediocin SJ-1 and nisin
21
Schved, F., Institute of Technology and Storage of Agricultural Products, Agricultural Research Organization, The Volcani Centre, Bet-Dagan, Israel
Henis, Y., Department of Plant Pathology and Microbiology, the Otto Warburg Centre for Biotechnology in Agriculture, The Hebrew University of Jerusalem, Rehovot, Israel
Juven, B.J., Institute of Technology and Storage of Agricultural Products, Agricultural Research Organization, The Volcani Centre, Bet-Dagan, Israel
Response of spheroplasts and chelator-permeabilized cells of Gram-negative bacteria to the action of the bacteriocins pediocin SJ-1 and nisin
We have attempted to bypass the outer membrane (OM) barrier of Escherichia coli and Salmonella typhimurium with pediocin SJ-1 (as compared with nisin) using chelating agents as OM permeabilizers. EDTA, and to less extent EGTA, enabled nisin, but not pediocin SJ-1, to permeate the cell OM of E. coli, to have access to the cytoplasmic membrane and to cause subsequent permeability changes, indicated by an increase in ANS fluorescence intensity and a shift of its emission maximum. Such spectral changes did not occur when, prior to addition, EDTA was saturated with Ca2+ and Mg2+. ANS fluorescence data indicated that, in spite of the fact that pediocin SJ-1 did traverse the EDTA-permeabilized OM of E. coli, it did not cause perturbation of its cytoplasmic membrane and was, therefore, unable to cause cell death. Spheroplasts prepared from E. coli were lysed when treated with nisin but not with pediocin SJ-1. We suggest that the resistance of Gram-negative bacteria to pediocin SJ-1 is due not only to this material's inability to permeate the OM but also (in contrast to nisin) to its inability to interact with the cytoplasmic membrane. © 1994.
Scientific Publication
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