BIOMAT Database Logo BIOMAT Database Logo

Mechanisms of action of bactericidal/permeability-increasing protein BPI on reconstituted outer membranes of gram-negative bacteria. 1997

A Wiese, and K Brandenburg, and S F Carroll, and E T Rietschel, and U Seydel
Department of Immunochemistry and Biochemical Microbiology, Center for Medicine and Biosciences, Research Center Borstel, Parkallee 10, D-23845 Borstel, Germany.

The mechanisms of interaction of the recombinant N-terminal portion of bactericidal/permeability-increasing protein, rBPI21, with various planar asymmetric and symmetric bilayer membranes, including the lipid matrix of the outer membrane of Gram-negative bacteria, were investigated via electrical measurements. For the lipopolysaccharide (LPS) leaflet of the outer membrane, isolated deep rough mutant LPS of Escherichia coli strain F515 (F515 LPS) and Proteus mirabilis strain R45 (R45 LPS) were used. The addition of rBPI21 to the LPS side of asymmetric LPS/phospholipid membranes, as well as to black lipid membranes made from dioleoylphosphatidylglycerol (DOPG), led to membrane rupture. The innermembrane potential difference resulted in a slight increase from 0 to 5 mV for symmetric DOPG membranes but changed for asymmetric F515 LPS/PL membranes from -36 to +8 mV and for R45 LPS/PL membranes from -37 to -5 mV following the addition of rBPI21. In all cases, the addition of rBPI21 led to an increase in membrane current. The effect of rBPI21 on the innermembrane potential difference of LPS/PL membranes was significantly reduced in the presence of 40 mM MgCl2 (shift from -36 to -31 mV for F515 LPS). On the basis of these results and from our studies on the interaction of rBPI21 with lipid monolayers and aggregates [Wiese, A., et al. (1997) Biochemistry 36, 10301-10310], a model is discussed explaining how the observed membrane rupture, increase of membrane current, and change of transmembrane potential as induced by rBPI21 may contribute to bacterial dysfunction.

UI MeSH Term Description Entries
D008564 Membrane Potentials The voltage differences across a membrane. For cellular membranes they are computed by subtracting the voltage measured outside the membrane from the voltage measured inside the membrane. They result from differences of inside versus outside concentration of potassium, sodium, chloride, and other ions across cells' or ORGANELLES membranes. For excitable cells, the resting membrane potentials range between -30 and -100 millivolts. Physical, chemical, or electrical stimuli can make a membrane potential more negative (hyperpolarization), or less negative (depolarization). Resting Potentials,Transmembrane Potentials,Delta Psi,Resting Membrane Potential,Transmembrane Electrical Potential Difference,Transmembrane Potential Difference,Difference, Transmembrane Potential,Differences, Transmembrane Potential,Membrane Potential,Membrane Potential, Resting,Membrane Potentials, Resting,Potential Difference, Transmembrane,Potential Differences, Transmembrane,Potential, Membrane,Potential, Resting,Potential, Transmembrane,Potentials, Membrane,Potentials, Resting,Potentials, Transmembrane,Resting Membrane Potentials,Resting Potential,Transmembrane Potential,Transmembrane Potential Differences
D008565 Membrane Proteins Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors. Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D001798 Blood Proteins Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of proteins. Blood Protein,Plasma Protein,Plasma Proteins,Serum Protein,Serum Proteins,Protein, Blood,Protein, Plasma,Protein, Serum,Proteins, Blood,Proteins, Plasma,Proteins, Serum
D002462 Cell Membrane The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells. Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D006090 Gram-Negative Bacteria Bacteria which lose crystal violet stain but are stained pink when treated by Gram's method. Gram Negative Bacteria
D000900 Anti-Bacterial Agents Substances that inhibit the growth or reproduction of BACTERIA. Anti-Bacterial Agent,Anti-Bacterial Compound,Anti-Mycobacterial Agent,Antibacterial Agent,Antibiotics,Antimycobacterial Agent,Bacteriocidal Agent,Bacteriocide,Anti-Bacterial Compounds,Anti-Mycobacterial Agents,Antibacterial Agents,Antibiotic,Antimycobacterial Agents,Bacteriocidal Agents,Bacteriocides,Agent, Anti-Bacterial,Agent, Anti-Mycobacterial,Agent, Antibacterial,Agent, Antimycobacterial,Agent, Bacteriocidal,Agents, Anti-Bacterial,Agents, Anti-Mycobacterial,Agents, Antibacterial,Agents, Antimycobacterial,Agents, Bacteriocidal,Anti Bacterial Agent,Anti Bacterial Agents,Anti Bacterial Compound,Anti Bacterial Compounds,Anti Mycobacterial Agent,Anti Mycobacterial Agents,Compound, Anti-Bacterial,Compounds, Anti-Bacterial
D023181 Antimicrobial Cationic Peptides Small cationic peptides that are an important component, in most species, of early innate and induced defenses against invading microbes. In animals they are found on mucosal surfaces, within phagocytic granules, and on the surface of the body. They are also found in insects and plants. Among others, this group includes the DEFENSINS, protegrins, tachyplesins, and thionins. They displace DIVALENT CATIONS from phosphate groups of MEMBRANE LIPIDS leading to disruption of the membrane. Cationic Antimicrobial Peptide,Cationic Antimicrobial Peptides,Cationic Host Defense Peptides,Host Defense Peptide,Microbicidal Cationic Proteins,Amphipathic Cationic Antimicrobial Peptides,Host Defense Peptides,Antimicrobial Peptide, Cationic,Antimicrobial Peptides, Cationic,Cationic Peptides, Antimicrobial,Cationic Proteins, Microbicidal,Defense Peptide, Host,Defense Peptides, Host,Peptide, Cationic Antimicrobial,Peptide, Host Defense,Peptides, Antimicrobial Cationic,Peptides, Cationic Antimicrobial,Peptides, Host Defense,Proteins, Microbicidal Cationic

Related Publications

A Wiese, and K Brandenburg, and S F Carroll, and E T Rietschel, and U Seydel
The bactericidal/permeability-increasing protein (BPI), a potent element in host-defense against gram-negative bacteria and lipopolysaccharide.
April 1993, Immunobiology,
A Wiese, and K Brandenburg, and S F Carroll, and E T Rietschel, and U Seydel
The outer membrane permeability of Gram-negative bacteria: determination of permeability rate in reconstituted vesicle membranes.
October 1979, FEBS letters,
A Wiese, and K Brandenburg, and S F Carroll, and E T Rietschel, and U Seydel
Bactericidal/permeability-increasing protein (BPI) and lipopolysaccharide-binding protein (LBP): structure, function and regulation in host defence against Gram-negative bacteria.
August 2003, Biochemical Society transactions,
A Wiese, and K Brandenburg, and S F Carroll, and E T Rietschel, and U Seydel
Bactericidal permeability-increasing protein in host defence against gram-negative bacteria and endotoxin.
January 1994, Ciba Foundation symposium,
A Wiese, and K Brandenburg, and S F Carroll, and E T Rietschel, and U Seydel
Bactericidal/permeability increasing protein and host defense against gram-negative bacteria and endotoxin.
February 1993, Current opinion in immunology,
A Wiese, and K Brandenburg, and S F Carroll, and E T Rietschel, and U Seydel
Bactericidal/permeability-increasing protein (BPI) and BPI homologs at mucosal sites.
November 2008, Trends in immunology,
A Wiese, and K Brandenburg, and S F Carroll, and E T Rietschel, and U Seydel
The antiangiogenic properties of bactericidal/permeability-increasing protein (BPI).
January 2002, Annals of medicine,
A Wiese, and K Brandenburg, and S F Carroll, and E T Rietschel, and U Seydel
Bactericidal Permeability-Increasing Protein (BPI) Inhibits Mycobacterium tuberculosis Growth.
April 2024, Biomolecules,
A Wiese, and K Brandenburg, and S F Carroll, and E T Rietschel, and U Seydel
Outer membranes of gram-negative bacteria.
December 1987, Biochemical Society transactions,
A Wiese, and K Brandenburg, and S F Carroll, and E T Rietschel, and U Seydel
Murine bactericidal/permeability-increasing protein inhibits the endotoxic activity of lipopolysaccharide and gram-negative bacteria.
June 2008, Journal of immunology (Baltimore, Md. : 1950),
Copied contents to your clipboard!