Mechanisms of Action of Rabbit CAP18 on Monolayers and Liposomes Made from Endotoxins or Phospholipids

Gutsmann, T. ; Fix, M. ; Larrick, J.W. ; Wiese, A.
Springer
Published 2000
ISSN:
1432-1424
Keywords:
Key words: CAP18—Monolayer—Liposomes—Outer membrane—Lipopolysaccharide—Resistance
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Chemistry and Pharmacology
Notes:
Abstract. We have investigated the mechanism of action of the cationic antimicrobial protein (18 kDa) CAP18 on liposomes and monolayers made from phospholipids and enterobacterial lipopolysaccharides (LPS). CAP18 intercalates into lipid matrices composed of LPS from sensitive strains, weaker into those made of LPS from a resistant strain (Proteus mirabilis strain R45) or negatively charged phospholipids, but not into those composed of neutral phosphatidylcholine. From the combination of data obtained with fluorescence resonance energy transfer and Fourier-transform infrared spectroscopy and film balance measurements, it can be concluded that structural differences in the LPS determine the depth of intercalation of CAP18 into the respective lipid matrices. Thus, we identified the L-Arap4N linked to the first Kdo of the LPS of P. mirabilis strain R45 to be responsible for the CAP18 resistance of this strain. These data provide insight into CAP18-mediated effects on the integrity of the outer membrane of Gram-negative bacteria and led to an improved model for rabbit CAP18 membrane interaction.
Type of Medium:
Electronic Resource
URL:
_version_ 1798295677867917312
autor Gutsmann, T.
Fix, M.
Larrick, J.W.
Wiese, A.
autorsonst Gutsmann, T.
Fix, M.
Larrick, J.W.
Wiese, A.
book_url http://dx.doi.org/10.1007/s00232001092
datenlieferant nat_lic_papers
hauptsatz hsatz_simple
identnr NLM207056803
issn 1432-1424
journal_name The journal of membrane biology
materialart 1
notes Abstract. We have investigated the mechanism of action of the cationic antimicrobial protein (18 kDa) CAP18 on liposomes and monolayers made from phospholipids and enterobacterial lipopolysaccharides (LPS). CAP18 intercalates into lipid matrices composed of LPS from sensitive strains, weaker into those made of LPS from a resistant strain (Proteus mirabilis strain R45) or negatively charged phospholipids, but not into those composed of neutral phosphatidylcholine. From the combination of data obtained with fluorescence resonance energy transfer and Fourier-transform infrared spectroscopy and film balance measurements, it can be concluded that structural differences in the LPS determine the depth of intercalation of CAP18 into the respective lipid matrices. Thus, we identified the L-Arap4N linked to the first Kdo of the LPS of P. mirabilis strain R45 to be responsible for the CAP18 resistance of this strain. These data provide insight into CAP18-mediated effects on the integrity of the outer membrane of Gram-negative bacteria and led to an improved model for rabbit CAP18 membrane interaction.
package_name Springer
publikationsjahr_anzeige 2000
publikationsjahr_facette 2000
publikationsjahr_intervall 7999:2000-2004
publikationsjahr_sort 2000
publisher Springer
reference 176 (2000), S. 223-236
schlagwort Key words: CAP18—Monolayer—Liposomes—Outer membrane—Lipopolysaccharide—Resistance
search_space articles
shingle_author_1 Gutsmann, T.
Fix, M.
Larrick, J.W.
Wiese, A.
shingle_author_2 Gutsmann, T.
Fix, M.
Larrick, J.W.
Wiese, A.
shingle_author_3 Gutsmann, T.
Fix, M.
Larrick, J.W.
Wiese, A.
shingle_author_4 Gutsmann, T.
Fix, M.
Larrick, J.W.
Wiese, A.
shingle_catch_all_1 Gutsmann, T.
Fix, M.
Larrick, J.W.
Wiese, A.
Mechanisms of Action of Rabbit CAP18 on Monolayers and Liposomes Made from Endotoxins or Phospholipids
Key words: CAP18—Monolayer—Liposomes—Outer membrane—Lipopolysaccharide—Resistance
Key words: CAP18—Monolayer—Liposomes—Outer membrane—Lipopolysaccharide—Resistance
Abstract. We have investigated the mechanism of action of the cationic antimicrobial protein (18 kDa) CAP18 on liposomes and monolayers made from phospholipids and enterobacterial lipopolysaccharides (LPS). CAP18 intercalates into lipid matrices composed of LPS from sensitive strains, weaker into those made of LPS from a resistant strain (Proteus mirabilis strain R45) or negatively charged phospholipids, but not into those composed of neutral phosphatidylcholine. From the combination of data obtained with fluorescence resonance energy transfer and Fourier-transform infrared spectroscopy and film balance measurements, it can be concluded that structural differences in the LPS determine the depth of intercalation of CAP18 into the respective lipid matrices. Thus, we identified the L-Arap4N linked to the first Kdo of the LPS of P. mirabilis strain R45 to be responsible for the CAP18 resistance of this strain. These data provide insight into CAP18-mediated effects on the integrity of the outer membrane of Gram-negative bacteria and led to an improved model for rabbit CAP18 membrane interaction.
1432-1424
14321424
Springer
shingle_catch_all_2 Gutsmann, T.
Fix, M.
Larrick, J.W.
Wiese, A.
Mechanisms of Action of Rabbit CAP18 on Monolayers and Liposomes Made from Endotoxins or Phospholipids
Key words: CAP18—Monolayer—Liposomes—Outer membrane—Lipopolysaccharide—Resistance
Key words: CAP18—Monolayer—Liposomes—Outer membrane—Lipopolysaccharide—Resistance
Abstract. We have investigated the mechanism of action of the cationic antimicrobial protein (18 kDa) CAP18 on liposomes and monolayers made from phospholipids and enterobacterial lipopolysaccharides (LPS). CAP18 intercalates into lipid matrices composed of LPS from sensitive strains, weaker into those made of LPS from a resistant strain (Proteus mirabilis strain R45) or negatively charged phospholipids, but not into those composed of neutral phosphatidylcholine. From the combination of data obtained with fluorescence resonance energy transfer and Fourier-transform infrared spectroscopy and film balance measurements, it can be concluded that structural differences in the LPS determine the depth of intercalation of CAP18 into the respective lipid matrices. Thus, we identified the L-Arap4N linked to the first Kdo of the LPS of P. mirabilis strain R45 to be responsible for the CAP18 resistance of this strain. These data provide insight into CAP18-mediated effects on the integrity of the outer membrane of Gram-negative bacteria and led to an improved model for rabbit CAP18 membrane interaction.
1432-1424
14321424
Springer
shingle_catch_all_3 Gutsmann, T.
Fix, M.
Larrick, J.W.
Wiese, A.
Mechanisms of Action of Rabbit CAP18 on Monolayers and Liposomes Made from Endotoxins or Phospholipids
Key words: CAP18—Monolayer—Liposomes—Outer membrane—Lipopolysaccharide—Resistance
Key words: CAP18—Monolayer—Liposomes—Outer membrane—Lipopolysaccharide—Resistance
Abstract. We have investigated the mechanism of action of the cationic antimicrobial protein (18 kDa) CAP18 on liposomes and monolayers made from phospholipids and enterobacterial lipopolysaccharides (LPS). CAP18 intercalates into lipid matrices composed of LPS from sensitive strains, weaker into those made of LPS from a resistant strain (Proteus mirabilis strain R45) or negatively charged phospholipids, but not into those composed of neutral phosphatidylcholine. From the combination of data obtained with fluorescence resonance energy transfer and Fourier-transform infrared spectroscopy and film balance measurements, it can be concluded that structural differences in the LPS determine the depth of intercalation of CAP18 into the respective lipid matrices. Thus, we identified the L-Arap4N linked to the first Kdo of the LPS of P. mirabilis strain R45 to be responsible for the CAP18 resistance of this strain. These data provide insight into CAP18-mediated effects on the integrity of the outer membrane of Gram-negative bacteria and led to an improved model for rabbit CAP18 membrane interaction.
1432-1424
14321424
Springer
shingle_catch_all_4 Gutsmann, T.
Fix, M.
Larrick, J.W.
Wiese, A.
Mechanisms of Action of Rabbit CAP18 on Monolayers and Liposomes Made from Endotoxins or Phospholipids
Key words: CAP18—Monolayer—Liposomes—Outer membrane—Lipopolysaccharide—Resistance
Key words: CAP18—Monolayer—Liposomes—Outer membrane—Lipopolysaccharide—Resistance
Abstract. We have investigated the mechanism of action of the cationic antimicrobial protein (18 kDa) CAP18 on liposomes and monolayers made from phospholipids and enterobacterial lipopolysaccharides (LPS). CAP18 intercalates into lipid matrices composed of LPS from sensitive strains, weaker into those made of LPS from a resistant strain (Proteus mirabilis strain R45) or negatively charged phospholipids, but not into those composed of neutral phosphatidylcholine. From the combination of data obtained with fluorescence resonance energy transfer and Fourier-transform infrared spectroscopy and film balance measurements, it can be concluded that structural differences in the LPS determine the depth of intercalation of CAP18 into the respective lipid matrices. Thus, we identified the L-Arap4N linked to the first Kdo of the LPS of P. mirabilis strain R45 to be responsible for the CAP18 resistance of this strain. These data provide insight into CAP18-mediated effects on the integrity of the outer membrane of Gram-negative bacteria and led to an improved model for rabbit CAP18 membrane interaction.
1432-1424
14321424
Springer
shingle_title_1 Mechanisms of Action of Rabbit CAP18 on Monolayers and Liposomes Made from Endotoxins or Phospholipids
shingle_title_2 Mechanisms of Action of Rabbit CAP18 on Monolayers and Liposomes Made from Endotoxins or Phospholipids
shingle_title_3 Mechanisms of Action of Rabbit CAP18 on Monolayers and Liposomes Made from Endotoxins or Phospholipids
shingle_title_4 Mechanisms of Action of Rabbit CAP18 on Monolayers and Liposomes Made from Endotoxins or Phospholipids
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timestamp 2024-05-06T09:40:01.092Z
titel Mechanisms of Action of Rabbit CAP18 on Monolayers and Liposomes Made from Endotoxins or Phospholipids
titel_suche Mechanisms of Action of Rabbit CAP18 on Monolayers and Liposomes Made from Endotoxins or Phospholipids
topic W
V
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