Cited by 1,879Bacterial Genetics and BiotechnologyAntimicrobial Peptides and ActivitiesAntimicrobial agents and applications

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Agents that increase the permeability of the outer membrane

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Vaara, M·1992·Microbiological Reviews

DOI 10.1128/mr.56.3.395-411.1992PMC PMC372877

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Abstract

The outer membrane of gram-negative bacteria provides the cell with an effective permeability barrier against external noxious agents, including antibiotics, but is itself a target for antibacterial agents such as polycations and chelators. Both groups of agents weaken the molecular interactions of the lipopolysaccharide constituent of the outer membrane. Various polycations are able, at least under certain conditions, to bind to the anionic sites of lipopolysaccharide. Many of these disorganize and cross the outer membrane and render it permeable to drugs which permeate the intact membrane very poorly. These polycations include polymyxins and their derivatives, protamine, polymers of basic amino acids, compound 48/80, insect cecropins, reptilian magainins, various cationic leukocyte peptides (defensins, bactenecins, bactericidal/permeability-increasing protein, and others), aminoglycosides, and many more. However, the cationic character is not the sole determinant required for the permeabilizing activity, and therefore some of the agents are much more effective permeabilizers than others. They are useful tools in studies in which the poor permeability of the outer membrane poses problems. Some of them undoubtedly have a role as natural antibiotic substances, and they or their derivatives might have some potential as pharmaceutical agents in antibacterial therapy as well. Also, chelators (such as EDTA, nitrilotriacetic acid, and sodium hexametaphosphate), which disintegrate the outer membrane by removing Mg2+ and Ca2+, are effective and valuable permeabilizers.

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Nikaido, H., & Vaara, M. (1985) · Microbiological Reviews · doi:10.1128/mr.49.1.1-32.1985 · Cited by 2,458
Self-citation
Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor.
Zasloff, M. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.15.5449 · Cited by 2,305
Structure and Function of Lipopolysaccharide Binding Protein
Schumann, R. R., Leong, S. R., Flaggs, G., Gray, P. W., Wright, S. D., Mathison, J. C., Tobias, P. S., & Ulevitch, R. J. (1990) · Science · doi:10.1126/science.2402637 · Cited by 1,672
The Release of Enzymes from Escherichia coli by Osmotic Shock and during the Formation of Spheroplasts
Neu, H. C., & HEPPEL, L. A. (1965) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97200-5 · Cited by 1,464
Defensins. Natural peptide antibiotics of human neutrophils.
Ganz, T., Selsted, M. E., Szklarek, D., Harwig, S. S. L., Daher, K. A., Bainton, D. F., & Lehrer, R. I. (1985) · Journal of Clinical Investigation · doi:10.1172/jci112120 · Cited by 1,416
Insect Immunity. Purification and Properties of Three Inducible Bactericidal Proteins from Hemolymph of Immunized Pupae of Hyalophora cecropia
Hultmark, D., Steiner, H., Rasmuson, T., & Boman, H. G. (1980) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1980.tb05991.x · Cited by 1,007
Polymyxin and Related Peptide Antibiotics
Storm, D. R., Rosenthal, K. S., & Swanson, P. E. (1977) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.46.070177.003451 · Cited by 759
Molecular architecture and functioning of the outer membrane of Escherichia coli and other gram-negative bacteria
Lugtenberg, B. J. J., & van Alphen, L. (1983) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(83)90014-x · Cited by 742
Interaction of human defensins with Escherichia coli. Mechanism of bactericidal activity.
Lehrer, R. I., Barton, A. P., Daher, K. A., Harwig, S. S. L., Ganz, T., & Selsted, M. E. (1989) · Journal of Clinical Investigation · doi:10.1172/jci114198 · Cited by 727
All-D amino acid-containing channel-forming antibiotic peptides.
Wade, D. C., Boman, A., Wåhlin, B., Drain, C. M., Andreu, D., Boman, H. G., & Merrifield, R. B. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.12.4761 · Cited by 677
The Outer Membrane of Gram-negative Bacteria
Nikaido, H., & Nakae, T. (1980) · Advances in microbial physiology/Advances in Microbial Physiology · doi:10.1016/s0065-2911(08)60208-8 · Cited by 588
PEPTIDES FROM FROG SKIN
Bevins, C. L., & ZASLOFF, M. A. (1990) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.59.070190.002143 · Cited by 584
Antibacterial peptides: Key components needed in immunity
Boman, H. G. (1991) · Cell · doi:10.1016/0092-8674(91)90154-q · Cited by 569
ALTERATIONS IN OUTER MEMBRANE PERMEABILITY
Hancock, R. E. W. (1984) · Annual Review of Microbiology · doi:10.1146/annurev.mi.38.100184.001321 · Cited by 567
Damage of the outer membrane of enteric gram-negative bacteria by lactoferrin and transferrin
Ellison, R. T., Giehl, T. J., & LaForce, F. M. (1988) · Infection and Immunity · doi:10.1128/iai.56.11.2774-2781.1988 · Cited by 540
Antimicrobial defensin peptides form voltage-dependent ion-permeable channels in planar lipid bilayer membranes.
Kagan, B. L., Selsted, M. E., Ganz, T., & Lehrer, R. I. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.1.210 · Cited by 532
Tachyplesin, a class of antimicrobial peptide from the hemocytes of the horseshoe crab (Tachypleus tridentatus). Isolation and chemical structure.
Nakamura, T., Furunaka, H., Miyata, T., Tokunaga, F., Muta, T., Iwanaga, S., Niwa, M., Takao, T., & Shimonishi, Y. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)37448-9 · Cited by 531
THE BARRIER FUNCTION OF THE GRAM‐NEGATIVE ENVELOPE
Leive, L. (1974) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1974.tb43261.x · Cited by 514
Channel-forming properties of cecropins and related model compounds incorporated into planar lipid membranes.
Christensen, B., Fink, J., Merrifield, R. B., & Mauzerall, D. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.14.5072 · Cited by 514
Use of the fluorescent probe 1-N-phenylnaphthylamine to study the interactions of aminoglycoside antibiotics with the outer membrane of Pseudomonas aeruginosa
Loh, B. A., Grant, C. W. M., & Hancock, R. E. W. (1984) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.26.4.546 · Cited by 484
Release of lipopolysaccharide by EDTA treatment of E., coli
Leive, L. (1965) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(65)90191-9 · Cited by 470
Apidaecins: antibacterial peptides from honeybees.
Casteels, P., Ampè, C., Jacobs, F. H. H., Vaeck, M., & Tempst, P. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08368.x · Cited by 469
Outer membrane barrier as a mechanism of antimicrobial resistance
Nikaido, H. (1989) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.33.11.1831 · Cited by 464
Antimicrobial action of .EPSILON.-poly-L-lysine.
Shima, S., Matsuoka, H., IWAMOTO, T., & Sakai, H. (1984) · The Journal of Antibiotics · doi:10.7164/antibiotics.37.1449 · Cited by 463
Purification and characterization of a potent bactericidal and membrane active protein from the granules of human polymorphonuclear leukocytes.
Weiss, J. P., Elsbach, P., Olsson, I., & Odeberg, H. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40872-6 · Cited by 451
Insect immunity. Attacins, a family of antibacterial proteins from Hyalophora cecropia.
Hultmark, D., Engström, Å., Andersson, K., Steiner, H., Bennich, H., & Boman, H. G. (1983) · The EMBO Journal · doi:10.1002/j.1460-2075.1983.tb01465.x · Cited by 442
Antibacterial peptides from pig intestine: isolation of a mammalian cecropin.
Lee, J. Y., Boman, A., Sun, C., Andersson, M., Jörnvall, H., Mutt, V., & Boman, H. G. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.23.9159 · Cited by 436
Outer membrane of Salmonella typhimurium
Nikaido, H. (1976) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(76)90182-6 · Cited by 378
Outer membrane of Salmonella typhimurium: accessibility of phospholipid head groups to phospholipase C and cyanogen bromide activated dextran in the external medium
Kamio, Y., & Nikaido, H. (1976) · Biochemistry · doi:10.1021/bi00657a012 · Cited by 378
Antimicrobial activity of synthetic magainin peptides and several analogues.
Zasloff, M., Martin, B., & Chen, H. C. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.3.910 · Cited by 371
Electrodialysis of Lipopolysaccharides and Their Conversion to Uniform Salt Forms
Galanos, C., & Luderitz, O. (1975) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1975.tb04172.x · Cited by 362
Antibiotic magainins exert cytolytic activity against transformed cell lines through channel formation.
Cruciani, R. A., Barker, J. L., ZASLOFF, M. A., Chen, H. C., & Colamonici, O. R. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.9.3792 · Cited by 362
Identification of a Lipid A Binding Site in the Acute Phase Reactant Lipopolysaccharide Binding Protein
Tobias, P. S., Soldau, K., & Ulevitch, R. J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)81700-8 · Cited by 352
Defensins: Endogenous antibiotic peptides of animal cells
Lehrer, R. I., Ganz, T., & Selsted, M. E. (1991) · Cell · doi:10.1016/0092-8674(91)90632-9 · Cited by 345
Interaction of divalent cations and polymyxin B with lipopolysaccharide
Schindler, M., & Osborn, M. (1979) · Biochemistry · doi:10.1021/bi00587a024 · Cited by 336
Insect immunity: isolation from immune blood of the dipteran Phormia terranovae of two insect antibacterial peptides with sequence homology to rabbit lung macrophage bactericidal peptides.
Lambert, J., Keppi, E., Dimarcq, J. L., Wicker, C., Reichhart, J., Dunbar, B., Lepage, P., DORSSELAER, A. V., Hoffmann, J. A., & Fothergill, J. E. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.1.262 · Cited by 324
Antibacterial and antimalarial properties of peptides that are cecropin‐melittin hybrids
Boman, H. G., Wade, D. C., Boman, I. A., Wåhlin, B., & Merrifield, R. B. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)81505-4 · Cited by 314
Purification and antibacterial activity of antimicrobial peptides of rabbit granulocytes
Selsted, M. E., Szklarek, D., & Lehrer, R. I. (1984) · Infection and Immunity · doi:10.1128/iai.45.1.150-154.1984 · Cited by 306
Isolation and characterization of abaecin, a major antibacterial response peptide in the honeybee (Apis mellifera)
Casteels, P., Ampè, C., Riviere, L. R., van Damme, J., Elicone, C., Fleming, M. D., JACOBS, F., & Tempst, P. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb15315.x · Cited by 305
Purification, composition, and activity of two bactenecins, antibacterial peptides of bovine neutrophils
Gennaro, R., Skerlavaj, B., & Romeo, D. (1989) · Infection and Immunity · doi:10.1128/iai.57.10.3142-3146.1989 · Cited by 300
Antimicrobial Peptides, Isolated from Horseshoe Crab Hemocytes, Tachyplesin II, and Polyphemusins I and II: Chemical Structures and Biological Activity1
Miyata, T., Tokunaga, F., Yoneya, T., Yoshikawa, K., Iwanaga, S., Niwa, M., Takao, T., & Shimonishi, Y. (1989) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a122913 · Cited by 294
All‐D‐magainin: chirality, antimicrobial activity and proteolytic resistance
Bessalle, R., Kapitkovsky, A., Gorea, A., Shalit, I., & Fridkin, M. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)81351-n · Cited by 294
Antibacterial properties of eosinophil major basic protein and eosinophil cationic protein.
Lehrer, R., Szklarek, D., Barton, A. P., Ganz, T., Hamann, K. J., & Gleich, G. J. (1989) · The Journal of Immunology · doi:10.4049/jimmunol.142.12.4428 · Cited by 292
Compounds which increase the permeability of the Pseudomonas aeruginosa outer membrane
Hancock, R. E. W., & Wong, P. G. (1984) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.26.1.48 · Cited by 286
Lysis of gram-negative organisms and the role of versene
Repaske, R. (1958) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(58)90044-1 · Cited by 279
Antibiotic proteins of human polymorphonuclear leukocytes.
Gabay, J. E., Scott, R., Campanelli, D., Griffith, J. E., Wilde, C., Marra, M. N., Seeger, M., & Nathan, C. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.14.5610 · Cited by 271
Bactericidal/permeability-increasing protein has endotoxin-neutralizing activity.
MARRA, M. N., WILDE, C. G., Griffith, J. E., Snable, J. L., & Scott, R. W. (1990) · The Journal of Immunology · doi:10.4049/jimmunol.144.2.662 · Cited by 270
Cell‐free immunity in Cecropia
Boman, H. G., Faye, I., Gudmundsson, G. H., Jong‐Youn, L. E. E., & Lidholm, D.-A. (1991) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1991.tb16252.x · Cited by 263
Routes of quinolone permeation in Escherichia coli
Chapman, J., & Georgopapadakou, N. H. (1988) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.32.4.438 · Cited by 254
Polycations as outer membrane-disorganizing agents
Vaara, M., & Vaara, T. (1983) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.24.1.114 · Cited by 252
Self-citation
Separation and purification of a potent bactericidal/permeability-increasing protein and a closely associated phospholipase A2 from rabbit polymorphonuclear leukocytes. Observations on their relationship.
Elsbach, P., Weiss, J. P., Franson, R. C., Beckerdite-Quagliata, S., Schneider, A., & Harris, L. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86622-x · Cited by 235
Interaction of polycationic antibiotics with Pseudomonas aeruginosa lipopolysaccharide and lipid A studied by using dansyl-polymyxin
Moore, R. A., Bates, N. C., & Hancock, R. E. W. (1986) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.29.3.496 · Cited by 235
Sensitization of Gram-negative bacteria to antibiotics and complement by a nontoxic oligopeptide
Vaara, M., & Vaara, T. (1983) · Nature · doi:10.1038/303526a0 · Cited by 232
Self-citation
Role of Lipopolysaccharides in Antibiotic Resistance and Bacteriophage Adsorption of Escherichia coli K-12
Tamaki, S., Sato, T., & Matsuhashi, M. (1971) · Journal of Bacteriology · doi:10.1128/jb.105.3.968-975.1971 · Cited by 230
Antimicrobial peptide magainin I from Xenopus skin forms anion-permeable channels in planar lipid bilayers
Duclohier, H., Molle, G., & Spach, G. (1989) · Biophysical Journal · doi:10.1016/s0006-3495(89)82746-8 · Cited by 222
Outer membrane protein H1 of Pseudomonas aeruginosa: involvement in adaptive and mutational resistance to ethylenediaminetetraacetate, polymyxin B, and gentamicin
Nicas, T. I., & Hancock, R. E. W. (1980) · Journal of Bacteriology · doi:10.1128/jb.143.2.872-878.1980 · Cited by 221
Involvement of the outer membrane in gentamicin and streptomycin uptake and killing in Pseudomonas aeruginosa
Hancock, R. E. W., Raffle, V. J., & Nicas, T. I. (1981) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.19.5.777 · Cited by 221
Azurocidin and a homologous serine protease from neutrophils. Differential antimicrobial and proteolytic properties.
Campanelli, D., Detmers, P., Nathan, C., & Gabay, J. E. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114518 · Cited by 216
Polycations sensitize enteric bacteria to antibiotics
Vaara, M., & Vaara, T. (1983) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.24.1.107 · Cited by 215
Self-citation
A family of lipopolysaccharide binding proteins involved in responses to gram-negative sepsis.
Tobias, P. S., Mathison, J. C., & Ulevitch, R. J. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68262-6 · Cited by 212
Concurrent assessment of inner and outer membrane permeabilization and bacteriolysis in E. coli by multiple-wavelength spectrophotometry
Lehrer, R. I., Barton, A. P., & Ganz, T. (1988) · Journal of Immunological Methods · doi:10.1016/0022-1759(88)90414-0 · Cited by 211
Cationic antimicrobial proteins isolated from human neutrophil granulocytes in the presence of diisopropyl fluorophosphate
Shafer, W. M., Martin, L., & Spitznagel, J. (1984) · Infection and Immunity · doi:10.1128/iai.45.1.29-35.1984 · Cited by 210
Actinomycin sensitivity in Escherichiacoli produced by EDTA
Leive, L. (1965) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(65)90874-0 · Cited by 207
Antimicrobial polypeptides of human neutrophils
Lehrer, R., & Ganz, T. (1990) · Blood · doi:10.1182/blood.v76.11.2169.bloodjournal76112169 · Cited by 206
Antibiotic uptake into gram-negative bacteria
Hancock, R. E. W., & Bell, A. (1988) · European Journal of Clinical Microbiology & Infectious Diseases · doi:10.1007/bf01975036 · Cited by 205
Rapid membrane permeabilization and inhibition of vital functions of gram-negative bacteria by bactenecins
Skerlavaj, B., Romeo, D., & Gennaro, R. (1990) · Infection and Immunity · doi:10.1128/iai.58.11.3724-3730.1990 · Cited by 202
Amino acid sequences of two proline-rich bactenecins. Antimicrobial peptides of bovine neutrophils.
Frank, R. W., Gennaro, R., Schneider, K., Przybylski, M., & Romeo, D. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30595-1 · Cited by 199
Cloning of the cDNA of a Human Neutrophil Bactericidal Protein
Gray, P. W., Flaggs, G., Leong, S. R., Gumina, R. J., Weiss, J. P., Ooi, C. E., & Elsbach, P. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60560-5 · Cited by 199
High state of order of isolated bacterial lipopolysaccharide and its possible contribution to the permeation barrier property of the outer membrane
Labischinski, H., Barnickel, G., Bradaczek, H., Naumann, D., Rietschel, E., & Giesbrecht, P. (1985) · Journal of Bacteriology · doi:10.1128/jb.162.1.9-20.1985 · Cited by 197
Characterization of the lipopolysaccharide from the polymyxin‐resistant pmrA mutants of Salmonella typhimurium
Vaara, M., Vaara, T., Jensen, M., Helander, I. M., Nurminen, M., Rietschel, E., & Mäkelä, P. H. (1981) · FEBS Letters · doi:10.1016/0014-5793(81)80777-6 · Cited by 195
Self-citation
Outer membranes of Gram‐negative bacteria are permeable to steroid probes
Plésiat, P., & Nikaido, H. (1992) · Molecular Microbiology · doi:10.1111/j.1365-2958.1992.tb00853.x · Cited by 191
Manipulation of intracellular magnesium content in polymyxin B nonapeptide-sensitized Escherichia coli by ionophore A23187
Alatossava, T., Jütte, H., Kühn, A., & Kellenberger, E. (1985) · Journal of Bacteriology · doi:10.1128/jb.162.1.413-419.1985 · Cited by 185
Endotoxin-neutralizing properties of the 25 kD N-terminal fragment and a newly isolated 30 kD C-terminal fragment of the 55-60 kD bactericidal/permeability-increasing protein of human neutrophils.
Ooi, C. E., Weiss, J. P., Doerfler, M. E., & Elsbach, P. (1991) · The Journal of Experimental Medicine · doi:10.1084/jem.174.3.649 · Cited by 181
Interaction of aminoglycosides with the outer membranes and purified lipopolysaccharide and OmpF porin of Escherichia coli
Hancock, R. E. W., Farmer, S. W., Li, Z. S., & Poole, K. (1991) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.35.7.1309 · Cited by 180
Isolation and Biological Activities of Limulus Anticoagulant (Anti-LPS Factor) which Interacts with Lipopolysaccharide (LPS)1
Morita, T., Ohtsubo, S., Nakamura, T., Tanaka, S., Iwanaga, S., Ohashi, K., & Niwa, M. (1985) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a135218 · Cited by 168
Lipopolysaccharide interaction with lysozyme
Ohno, N., & Morrison, D. C. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83761-9 · Cited by 165
Structural characterization of the lipid A component of Bacteroides fragilis strain NCTC 9343 lipopolysaccharide
Weintraub, A., Zähringer, U., Wollenweber, H. W., Seydel, U., & Rietschel, E. T. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb14945.x · Cited by 164
Purification, toxicity, and antiendotoxin activity of polymyxin B nonapeptide
Danner, R. L., Joiner, K. A., Rubin, M., Patterson, W. H., Johnson, N., AYERS, K. M., & Parrillo, J. E. (1989) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.33.9.1428 · Cited by 159
Antibiotic proteins of human neutrophils.
Spitznagel, J. K. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114851 · Cited by 158
Binding of polycationic antibiotics and polyamines to lipopolysaccharides of Pseudomonas aeruginosa
Peterson, A. A., Hancock, R. E. W., & McGroarty, E. J. (1985) · Journal of Bacteriology · doi:10.1128/jb.164.3.1256-1261.1985 · Cited by 156
Attacin, an antibacterial protein from Hyalophora cecropia, inhibits synthesis of outer membrane proteins in Escherichia coli by interfering with omp gene transcription
Carlsson, A., Engström, P., Palva, E. T., & Bennich, H. (1991) · Infection and Immunity · doi:10.1128/iai.59.9.3040-3045.1991 · Cited by 154
A 25-kDa NH2-terminal fragment carries all the antibacterial activities of the human neutrophil 60-kDa bactericidal/permeability-increasing protein.
Ooi, C. E., Weiss, J. P., Elsbach, P., Frangione, B., & Mannion, B. A. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48110-0 · Cited by 151
Primary structure of limulus anticoagulant anti-lipopolysaccharide factor.
Aketagawa, J., Miyata, T., Ohtsubo, S., Nakamura, T., Morita, T., Hayashida, H., Miyata, T., Iwanaga, S., Takao, T., & Shimonishi, Y. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38399-0 · Cited by 151
Interaction of macrophage cationic proteins with the outer membrane of Pseudomonas aeruginosa
Sawyer, J. G., Martin, N., & Hancock, R. E. W. (1988) · Infection and Immunity · doi:10.1128/iai.56.3.693-698.1988 · Cited by 151
Antibacterial agents specifically inhibiting lipopolysaccharide synthesis
Goldman, R. C., Kohlbrenner, W. E., Lartey, P. A., & Pernet, A. G. (1987) · Nature · doi:10.1038/329162a0 · Cited by 143
Chemical structure of the lipid A component of the lipopolysaccharide from a Proteus mirabilis Re‐mutant
Sidorczyk, Z., Zähringer, U., & Rietschel, E. (1983) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1983.tb07789.x · Cited by 141
The Effect of Defined Lipopolysaccharide Core Defects upon Antibiotic Resistances of Salmonella typhimurium
Roantree, R. J., Kuo, T. T., & MacPhee, D. G. (1977) · Journal of General Microbiology · doi:10.1099/00221287-103-2-223 · Cited by 138
Two mutations which affect the barrier function of the Escherichia coli K-12 outer membrane
Coleman, W. G., & Leive, L. (1979) · Journal of Bacteriology · doi:10.1128/jb.139.3.899-910.1979 · Cited by 137
Involvement of outer membrane of Pseudomonas cepacia in aminoglycoside and polymyxin resistance
Moore, R. A., & Hancock, R. E. W. (1986) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.30.6.923 · Cited by 133
Outer-Membrane Permeability of Bacteria
Nakae, T. (1986) · CRC Critical Reviews in Microbiology · doi:10.3109/10408418609108734 · Cited by 132
Role of permeability barriers in resistance to β-lactam antibiotics
Nikaido, H. (1985) · Pharmacology & Therapeutics · doi:10.1016/0163-7258(85)90069-5 · Cited by 131
Lactoferrin and transferrin damage of the Gram-negative outer membrane is modulated by Ca2+ and Mg2+
Ellison, R. T., LaForce, F. M., Giehl, T. J., Boose, D., & Dunn, B. E. (1990) · Journal of General Microbiology · doi:10.1099/00221287-136-7-1437 · Cited by 131
Mode of action of gramicidin S on Escherichia coli membrane
Katsu, T., Kobayashi, H., & Fujita, Y. (1986) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(86)90560-2 · Cited by 128
Antibacterial activity of microbicidal cationic proteins 1 and 2, natural peptide antibiotics of rabbit lung macrophages
Lehrer, R. I., Selsted, M. E., Szklarek, D., & Fleischmann, J. (1983) · Infection and Immunity · doi:10.1128/iai.42.1.10-14.1983 · Cited by 126
The antibacterial effect of attacins from the silk moth Hyalophora cecropia is directed against the outer membrane of Escherichia coli.
Engström, P., Carlsson, A., Engström, Å., Tao, Z., & Bennich, H. (1984) · The EMBO Journal · doi:10.1002/j.1460-2075.1984.tb02302.x · Cited by 122
Partial characterization and purification of a rabbit granulocyte factor that increases permeability of Escherichia coli.
Weiss, J. P., Franson, R. C., Beckerdite-Quagliata, S., Schmeidler, K., & Elsbach, P. (1975) · Journal of Clinical Investigation · doi:10.1172/jci107915 · Cited by 121
Mechanism of action of DuP 721: inhibition of an early event during initiation of protein synthesis
Eustice, D. C., Feldman, P., Zajac, I., & Slee, A. (1988) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.32.8.1218 · Cited by 118
Separation of sublethal and lethal effects of the bactericidal/permeability increasing protein on Escherichia coli.
Mannion, B. A., Weiss, J. P., & Elsbach, P. (1990) · Journal of Clinical Investigation · doi:10.1172/jci114512 · Cited by 116
Identification of the primary antimicrobial domains in human neutrophil cathepsin G.
Bangalore, N., Travis, J. W., Onunka, V. C., Pohl, J., & Shafer, W. M. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77388-2 · Cited by 115
Release of Surface Enzymes in Enterobacteriaceae by Osmotic Shock
Neu, H. C., & Chou, J. (1967) · Journal of Bacteriology · doi:10.1128/jb.94.6.1934-1945.1967 · Cited by 114
Outer Membrane Permeability Barrier Disruption by Polymyxin in Polymyxin-Susceptible and -Resistant Salmonella typhimurium
Vaara, M., & Vaara, T. (1981) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.19.4.578 · Cited by 113
Self-citation
Susceptibility of gram-negative bacteria to polymyxin B nonapeptide
Viljanen, P., & Vaara, M. (1984) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.25.6.701 · Cited by 112
Self-citation
Leakage of periplasmic proteins from Escherichia coli mediated by polymyxin B nonapeptide
DIXON, R. A., & Chopra, I. (1986) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.29.5.781 · Cited by 112
Investigation into the fluidity of lipopolysaccharide and free lipid A membrane systems by Fourier‐transform infrared spectroscopy and differential scanning calorimetry
Brandenburg, K., & Seydel, U. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb19114.x · Cited by 106
Mechanisms for the microbicidal activity of cationic proteins of human granulocytes
Odeberg, H., & Olsson, I. (1976) · Infection and Immunity · doi:10.1128/iai.14.6.1269-1275.1976 · Cited by 105
The lipid A biosynthesis mutation lpxA2 of Escherichia coli results in drastic antibiotic supersusceptibility
Vuorio, R., & Vaara, M. (1992) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.36.4.826 · Cited by 103
Self-citation
Permeability of lipopolysaccharide-deficient (rough) mutants of Salmonella typhimurium to antibiotics, lysozyme, and other agents
Sanderson, K. E., MacAlister, T. J., Costerton, J. W., & Cheng, K.-J. (1974) · Canadian Journal of Microbiology · doi:10.1139/m74-176 · Cited by 102
Primary Structure of Anti-Lipopolysaccharide Factor from American Horseshoe Crab, Limulus polyphemus1
Muta, T., Miyata, T., Tokunaga, F., Nakamura, T., & Iwanaga, S. (1987) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a121999 · Cited by 99
Ionizing groups in lipopolysaccharides of Pseudomonas cepacia in relation to antibiotic resistance
Cox, A. D., & Wilkinson, S. G. (1991) · Molecular Microbiology · doi:10.1111/j.1365-2958.1991.tb00735.x · Cited by 96
Binding of polymyxin B nonapeptide to gram-negative bacteria
Vaara, M., & Viljanen, P. (1985) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.27.4.548 · Cited by 96
Self-citation
Increased outer membrane resistance to ethylenediaminetetraacetate and cations in novel lipid A mutants
Vaara, M. (1981) · Journal of Bacteriology · doi:10.1128/jb.148.2.426-434.1981 · Cited by 94
Self-citation
Microbicidal mechanisms of human granulocytes: synergistic effects of granulocyte elastase and myeloperoxidase or chymotrypsin-like cationic protein
Odeberg, H., & Olsson, I. (1976) · Infection and Immunity · doi:10.1128/iai.14.6.1276-1283.1976 · Cited by 94
Polymyxin B and polymyxin B nonapeptide alter cytoplasmic membrane permeability in Escherichia coli
DIXON, R. A., & Chopra, I. (1986) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/18.5.557 · Cited by 94
Late intraphagosomal hydrogen ion concentration favors the in vitro antimicrobial capacity of a 37-kilodalton cationic granule protein of human neutrophil granulocytes
Shafer, W. M., Martin, L. E., & Spitznagel, J. K. (1986) · Infection and Immunity · doi:10.1128/iai.53.3.651-655.1986 · Cited by 93
Delta pH-dependent accumulation of tetracycline in Escherichia coli
Yamaguchi, A., Ohmori, H., Kaneko-Ohdera, M., Nomura, T., & Sawai, T. (1991) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.35.1.53 · Cited by 92
The role of lipopolysaccharides in the action of the bactericidal/permeability-increasing neutrophil protein on the bacterial envelope.
Weiss, J. P., Muello, K., Victor, M., & Elsbach, P. (1984) · The Journal of Immunology · doi:10.4049/jimmunol.132.6.3109 · Cited by 90
envM genes of Salmonella typhimurium and Escherichia coli
Turnowsky, F., Fuchs, K. P., Jeschek, C., & Högenauer, G. (1989) · Journal of Bacteriology · doi:10.1128/jb.171.12.6555-6565.1989 · Cited by 89
Decreased binding of antibiotics to lipopolysaccharides from polymyxin-resistant strains of Escherichia coli and Salmonella typhimurium
Peterson, A. A., Fesik, S. W., & McGroarty, E. J. (1987) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.31.2.230 · Cited by 89
Interactions between magainin 2 and Salmonella typhimurium outer membranes: effect of lipopolysaccharide structure
Rana, F. R., Macias, E. A., Sultany, C. M., Modzrakowski, M. C., & Blazyk, J. (1991) · Biochemistry · doi:10.1021/bi00238a008 · Cited by 86
The Chemical Structure of the Lipid A Component of Lipopolysaccharides from Chromobacterium violaceum NCTC 9694
Hase, S., & Rietschel, E. (1977) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1977.tb11500.x · Cited by 85
Role of Charge and Hydrophobic Interactions in the Action of Bactericidal/Permeability-increasing Protein of Neutrophils on Gram-negative Bacteria
Weiss, J. P., Victor, M., & Elsbach, P. (1983) · Journal of Clinical Investigation · doi:10.1172/jci110798 · Cited by 84
Outer Membrane Permeability of Pseudomonas aeruginosa
Nikaido, H., & HANCOCK, R. E. W. (1986) · Elsevier eBooks · doi:10.1016/b978-0-12-307210-8.50009-9 · Cited by 84
Correlation between renal membrane binding and nephrotoxicity of aminoglycosides
Williams, P. D., Bennett, D. B., Gleason, C. R., & Hottendorf, G. H. (1987) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.31.4.570 · Cited by 81
Purification, primary structure, and biological activity of guinea pig neutrophil cationic peptides
Yamashita, T., & Saito, K. (1989) · Infection and Immunity · doi:10.1128/iai.57.8.2405-2409.1989 · Cited by 81
Human lysosomal cathepsin G and granzyme B share a functionally conserved broad spectrum antibacterial peptide.
Shafer, W. M., Pohl, J., Onunka, V. C., Bangalore, N., & Travis, J. W. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52409-1 · Cited by 79
Decreased binding of polymyxin by polymyxin-resistant mutants of Salmonella typhimurium
Vaara, M., Vaara, T., & Sarvas, M. (1979) · Journal of Bacteriology · doi:10.1128/jb.139.2.664-667.1979 · Cited by 78
Self-citation
Antigonococcal activity of human neutrophil cathepsin G
Shafer, W. M., Onunka, V. C., & Martin, L. E. (1986) · Infection and Immunity · doi:10.1128/iai.54.1.184-188.1986 · Cited by 71
Amino acid sequence of CAP37, a human neutrophil granule‐derived antibacterial and monocyte‐specific chemotactic glycoprotein structurally similar to neutrophil elastase
Pohl, J., Pereira, H. A., Martin, N. M., & Spitznagel, J. K. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)80484-z · Cited by 71
EARLY AND DISCRETE CHANGES IN PERMEABILITY OF ESCHERICHIA COLI AND CERTAIN OTHER GRAM-NEGATIVE BACTERIA DURING KILLING BY GRANULOCYTES
Beckerdite-Quagliata, S., Mooney, C. L., Weiss, J. P., Franson, R., & Elsbach, P. (1974) · The Journal of Experimental Medicine · doi:10.1084/jem.140.2.396 · Cited by 71
Binding and neutralization of bacterial lipopolysaccharide by colistin nonapeptide
Warren, H. S., Kania, S. A., & Siber, G. R. (1985) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.28.1.107 · Cited by 67
Molecular cloning, sequencing, and characterization of cDNA for sarcotoxin IIA, an inducible antibacterial protein of Sarcophaga peregrina (flesh fly)
Ando, K., & Natori, S. (1988) · Biochemistry · doi:10.1021/bi00405a050 · Cited by 66
Preferential binding of the neutrophil cytoplasmic granule-derived bactericidal/permeability increasing protein to target bacteria. Implications and use as a means of purification.
Mannion, B. A., Kalatzis, E. S., Weiss, J. P., & Elsbach, P. (1989) · The Journal of Immunology · doi:10.4049/jimmunol.142.8.2807 · Cited by 63
Interaction of polymyxin B nonapeptide with anionic phospholipids
Kubesch, P., Boggs, J. M., Luciano, L., Maass, G., & Tuemmler, B. (1987) · Biochemistry · doi:10.1021/bi00382a012 · Cited by 62
Effects of Organic Cations on the Gram-negative Cell Wall and Their Bactericidal Activity with Ethylenediaminetetra-acetate and Surface Active Agents
Voss, J. G. (1967) · Journal of General Microbiology · doi:10.1099/00221287-48-3-391 · Cited by 61
Alteration Of Susceptibility To Edta, Polymyxin B And Gentamicin In Pseudomonas Aeruginosa By Divalent Cation Regulation Of Outer Membrane Protein H1
Nicas, T. I., & Hancock, R. E. W. (1983) · Microbiology · doi:10.1099/00221287-129-2-509 · Cited by 60
Fatty acid alterations and polymyxin B binding by lipopolysaccharides from Pseudomonas aeruginosa adapted to polymyxin B resistance
Conrad, R. S., & Galanos, C. (1989) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.33.10.1724 · Cited by 60
Influence of outer membrane mutations on susceptibility of Escherichia coli to the dibasic macrolide azithromycin
Farmer, S., Li, Z., & Hancock, R. E. W. (1992) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/29.1.27 · Cited by 60
Leakage of periplasmic enzymes from envA1 strains of Escherichia coli
Young, K., & Silver, L. L. (1991) · Journal of Bacteriology · doi:10.1128/jb.173.12.3609-3614.1991 · Cited by 59
Partitioning of hydrophobic probes into lipopolysaccharide bilayers
Vaara, M., Plachy, W. Z., & Nikaido, H. (1990) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/0005-2736(90)90218-d · Cited by 56
Self-citation
Pseudomonas aeruginosa outer membrane protein OprH: expression from the cloned gene and function in EDTA and gentamicin resistance
Bell, A., Bains, M., & Hancock, R. E. W. (1991) · Journal of Bacteriology · doi:10.1128/jb.173.21.6657-6664.1991 · Cited by 55
[Amino acid metabolism in larvae of the silkworm Bombyx mori].
Filippovich, I. B., & Bungova, V. G. (1968) · PubMed · Cited by 54
Salmonella typhimurium and Escherichia coli mutants with increased outer membrane permeability to hydrophobic compounds
Sukupolvi, S., & Vaara, M. (1989) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(89)90011-7 · Cited by 54
Self-citation
EFFECT OF POLYMYXIN ON THE LYSIS OF NEISSERIA CATARRHALIS BY LYSOZYME
Warren, G. H., Gray, J., & Yurchenco, J. A. (1957) · Journal of Bacteriology · doi:10.1128/jb.74.6.788-793.1957 · Cited by 53
Complementary DNA sequence of human neutrophil azurocidin, an antibiotic with extensive homology to serine proteases
de Almeida, R. P., Melchior, M., Campanelli, D., Nathan, C., & Gabay, J. E. (1991) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(91)91843-2 · Cited by 53
Polymyxin B octapeptide and polymyxin B heptapeptide are potent outer membrane permeability-increasing agents.
Kimura, Y., Matsunaga, H., & Vaara, M. (1992) · The Journal of Antibiotics · doi:10.7164/antibiotics.45.742 · Cited by 53
Self-citation
Sodium hexametaphosphate sensitizes Pseudomonas aeruginosa, several other species of Pseudomonas, and Escherichia coli to hydrophobic drugs
Vaara, M., & Jaakkola, J. J. K. (1989) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.33.10.1741 · Cited by 53
Self-citation
An outer membrane-disorganizing peptide PMBN sensitizes E. coli strains to serum bactericidal action.
Vaara, M., Viljanen, P., Vaara, T., & Mäkelä, P. H. (1984) · The Journal of Immunology · doi:10.4049/jimmunol.132.5.2582 · Cited by 52
Self-citation
Interaction of the Fluorescent Dye l-N-Phenylnaphthylamine with Escherichia coli Cells during Heat Stress and Recovery from Heat Stress
Tsuchido, T., Aoki, I., & Takano, M. (1989) · Microbiology · doi:10.1099/00221287-135-7-1941 · Cited by 52
Isolation and genetic characterization of polymyxin-resistant mutants of Salmonella
HELENAMAKELA, P., Sarvas, M., Calcagno, S., & Lounatmaa, K. (1978) · FEMS Microbiology Letters · doi:10.1016/0378-1097(78)90018-6 · Cited by 52
Isolation and genetic characterization of polymyxin-resistant mutants of Salmonella
Mäkelä, P. H., Sarvas, M., Calcagno, S., et al. (1978) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1978.tb01963.x · Cited by 51
In vitro cytotoxicity and antibiotic activity of polymyxin B nonapeptide
Duwe, A. K., Rupar, C. A., Horsman, G. B., & Vas, S. I. (1986) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.30.2.340 · Cited by 51
O antigen and lipid A phosphoryl groups in resistance of Salmonella typhimurium LT-2 to nonoxidative killing in human polymorphonuclear neutrophils
Stinavage, P., Martin, L. E., & Spitznagel, J. K. (1989) · Infection and Immunity · doi:10.1128/iai.57.12.3894-3900.1989 · Cited by 51
Novel antibiotic hypersensitive mutants ofEscherichia coligenetic mapping and chemical characterization
Clark, D. P. (1984) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1984.tb00209.x · Cited by 50
Defensins mediate the microbicidal activity of human neutrophil granule extract against Acinetobacter calcoaceticus
Greenwald, G. I., & Ganz, T. (1987) · Infection and Immunity · doi:10.1128/iai.55.6.1365-1368.1987 · Cited by 49
Chemical Synthesis, Isolation and Characterization of α-N-Fattyacyl Colistin Nonapeptide with Special Reference to the Correlation between Antimicrobial Activity and Carbon Number of Fattyacyl Moiety
Chihara, S., Ito, A., Yahata, M., Tobita, T., & Koyama, Y. (1974) · Agricultural and Biological Chemistry · doi:10.1271/bbb1961.38.521 · Cited by 49
The outer membrane permeability-increasing action of deacylpolymyxins.
Viljanen, P., Matsunaga, H., Kimura, Y., & Vaara, M. (1991) · The Journal of Antibiotics · doi:10.7164/antibiotics.44.517 · Cited by 49
Self-citation
Anti‐LPS factor in the horseshoe crab, Tachypleus tridentatus
Ohashi, K., Niwa, M., Nakamura, T., Morita, T., & Iwanaga, S. (1984) · FEBS Letters · doi:10.1016/0014-5793(84)80942-4 · Cited by 48
Secretion of alkaline phosphatase and phsopholipase C in Pseudomonas aeruginosa is specific and does not involve an increase in outer membrane permeability
Poole, K., & Hancock, R. E. W. (1983) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1983.tb00252.x · Cited by 48
Outer-Membrane Penetration Barriers as Components of Intrinsic Resistance to Beta-Lactam and Other Antibiotics in Escherichia coli K-12
Scudamore, R. A., Beveridge, T. J., & Goldner, M. (1979) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.15.2.182 · Cited by 48
Effect of small cationic leukocyte peptides (defensins) on the permeability barrier of the outer membrane
Viljanen, P., Koski, P., & Vaara, M. (1988) · Infection and Immunity · doi:10.1128/iai.56.9.2324-2329.1988 · Cited by 47
Self-citation
Disruption of the Escherichia coli outer membrane permeability barrier by immobilized polymyxin B.
Rosenthal, K. S., & Storm, D. R. (1977) · The Journal of Antibiotics · doi:10.7164/antibiotics.30.1087 · Cited by 47
Polymyxin B nonapeptide complexes with lipopolysaccharide
Vaara, M. (1983) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1983.tb00461.x · Cited by 45
Self-citation
Bactericidal cationic peptides involved in bacterial antagonism and host defence.
Hg, S. (1985) · PubMed · Cited by 45
Activation and Inactivation of Melittin Channels
Tosteson, M. T., & Tosteson, D. C. (1984) · Biophysical Journal · doi:10.1016/s0006-3495(84)84130-2 · Cited by 44
Escherichia coli susceptible to glycopeptide antibiotics
Shlaes, D. M., Shlaes, J. H., DAVIES, J. E., & Williamson, R. (1989) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.33.2.192 · Cited by 42
A synthetic 13-residue peptide corresponding to the hydrophobic region of bovine seminalplasmin has antibacterial activity and also causes lysis of red blood cells.
Sitaram, N., & Nagaraj, R. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)86965-4 · Cited by 41
Lipopolysaccharide structure determines ionic and hydrophobic binding of a cationic antimicrobial neutrophil granule protein
Farley, M. M., Shafer, W. M., & Spitznagel, J. K. (1988) · Infection and Immunity · doi:10.1128/iai.56.6.1589-1592.1988 · Cited by 41
Effects of lipopolysaccharide chemotype structure on binding and inactivation of hen egg lysozyme
Ohno, N., & Morrison, D. C. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb15252.x · Cited by 41
Sensitization by heat treatment of Escherichia coli K-12 cells to hydrophobic antibacterial compounds
Tsuchido, T., & Takano, M. (1988) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.32.11.1680 · Cited by 40
Detection of Agents That Alter the Bacterial Cell Surface
Sud, I. J., & FEINGOLD, D. S. (1975) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.8.1.34 · Cited by 39
Reconstitution of the lipid matrix of the outer membrane of Gram-negative bacteria as asymmetric planar bilayer
Seydel, U., Schröder, G., & Brandenburg, K. (1989) · The Journal of Membrane Biology · doi:10.1007/bf01870848 · Cited by 39
Repair of Injury in Freeze-Dried Salmonella anatum
Ray, B., Jezeski, J. J., & Busta, F. F. (1971) · Applied Microbiology · doi:10.1128/am.22.3.401-407.1971 · Cited by 38
Effect of ethylenediaminetetraacetate on phospholipids and outer membrane function in Escherichia coli
Hardaway, K. L., & Buller, C. S. (1979) · Journal of Bacteriology · doi:10.1128/jb.137.1.62-68.1979 · Cited by 37
EM49: A NEW POLYPEPTIDE ANTIBIOTIC ACTIVE AGAINST CELL MEMBRANES
Meyers, E., Parker, W. L., Brown, W. E., Linnett, P. E., & Strominger, J. L. (1974) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1974.tb43286.x · Cited by 37
Identification and sequence analysis of the gene mutated in the conditionally lethal outer membrane permeability mutant SS‐C of Salmonella typhimurium.
Hirvas, L., Koski, P., & Vaara, M. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb08036.x · Cited by 37
Self-citation
The Cell Envelope of Gram-Negative Bacteria: New Aspects of Its Function in Transport and Chemotaxis
Brass, J. M. (1986) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-71399-6_1 · Cited by 35
Effect of polymyxins on the lipopolysaccharide-defective mutants of Proteus mirabilis.
Kaca, W., Radziejewska‐Lebrecht, J., & Ur, B. (1990) · PubMed · Cited by 35
The ontogeny of a 57-Kd cationic antimicrobial protein of human polymorphonuclear leukocytes: localization to a novel granule population
Pereira, H., Spitznagel, J. K., Winton, E., Shafer, W. M., Martin, L., Guzman, G. S., Pohl, J., Scott, R., Marra, M. N., & Kinkade, J. J. (1990) · Blood · doi:10.1182/blood.v76.4.825.825 · Cited by 34
Inhibitory Effect of Sarcotoxin IIA, an Antibacterial Protein of Sarcophaga peregrina, on Growth of Escherichia coli1
Ando, K., & Natori, S. (1988) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a122337 · Cited by 34
The outer membrane permeability-increasing action of linear analogues of polymyxin B nonapeptide.
Vaara, M. (1991) · PubMed · Cited by 34
Self-citation
Comparison of granule proteins from human polymorphonuclear leukocytes which are bactericidal toward Pseudomonas aeruginosa
Wasiluk, K. R., Skubitz, K. M., & Gray, B. H. (1991) · Infection and Immunity · doi:10.1128/iai.59.11.4193-4200.1991 · Cited by 33
Comparative X‐ray and Fourier‐transform‐infrared investigations of conformational properties of bacterial and synthetic lipid A of Escherichia coli and Salmonella minnesota as well as partial structures and analogues thereof
Labischinski, H., Naumann, D., SCHULTZ, C., Kusumoto, S., Shiba, T., Rietschel, E., & Giesbrecht, P. (1989) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1989.tb14598.x · Cited by 32
The Pseudomonas aeruginosa Outer Membrane Permeability Barrier and How to Overcome It
Hancock, R. E. W. (2015) · Antibiotics and chemotherapy/Antibiotica et chemotherapia · doi:10.1159/000410475 · Cited by 31
Physiological effects of a bactericidal protein from human polymorphonuclear leukocytes on Pseudomonas aeruginosa
Hovde, C. J., & Gray, B. H. (1986) · Infection and Immunity · doi:10.1128/iai.52.1.90-95.1986 · Cited by 30
Increased outer membrane ornithine-containing lipid and lysozyme penetrability of Paracoccus denitrificans grown in a complex medium deficient in divalent cations
Wee, S., & Wilkinson, B. J. (1988) · Journal of Bacteriology · doi:10.1128/jb.170.7.3283-3286.1988 · Cited by 29
Ultrastructural Study of Salmonella typhimurium Treated with Membrane-Active Agents: Specific Reaction of Dansylchloride with Cell Envelope Components
Schindler, P. R. G., & Teuber, M. (1978) · Journal of Bacteriology · doi:10.1128/jb.135.1.198-206.1978 · Cited by 28
A highly efficient procedure for the quantitative formation of intact and viable lysozyme spheroplasts from escherichia coli
Marvin, H. J. P., & Witholt, B. (1987) · Analytical Biochemistry · doi:10.1016/0003-2697(87)90500-8 · Cited by 27
Dissipation of membrane potential of Escherichia coli cells induced by macromolecular polylysine
Katsu, T., Tsuchiya, T., & Fujita, Y. (1984) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(84)90489-3 · Cited by 27
The outer membrane as the penetration barrier against mupirocin in Gram-negative enteric bacteria
Vaara, M. (1992) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/29.2.221 · Cited by 27
Self-citation
Membrane-disorganizing property of polymyxin B nonapeptide
Lam, C., Hildebrandt, J., Schütze, E., & Wenzel, A. F. (1986) · Journal of Antimicrobial Chemotherapy · doi:10.1093/jac/18.1.9 · Cited by 25
Expression of H1 outer-membrane protein of Pseudomonas aeruginosa in relation to sensitivity to EDTA and polymyxin B
Said, A. A., Livermore, D. M., & Williams, R. J. (1987) · Journal of Medical Microbiology · doi:10.1099/00222615-24-3-267 · Cited by 24
Role of the Outer Membrane of Gram-Negative Bacteria in Antimicrobial Resistance
Nikaido, H. (1989) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-74095-4_1 · Cited by 23
Chain length heterogeneity of lipopolysaccharide released from Salmonella typhimurium by ethylenediaminetetraacetic acid or polycations
Hukari, R., Helander, I. M., & Vaara, M. (1986) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1986.tb09450.x · Cited by 23
Self-citation
Magainin-2 Releases Histamine from Rat Mast Cells
Hook, W. A., Tsuji, S., & Siraganian, R. P. (1990) · Experimental Biology and Medicine · doi:10.3181/00379727-193-42989 · Cited by 22
Mechanism of polymyxin B-mediated lysis of lipopolysaccharide-treated erythrocytes
Carr, C., & Morrison, D. C. (1985) · Infection and Immunity · doi:10.1128/iai.49.1.84-89.1985 · Cited by 21
Effect of defined lipopolysaccharide core defects on resistance of Salmonella typhimurium to freezing and thawing and other stresses
Bennett, G. M., Seaver, A., & Calcott, P. H. (1981) · Applied and Environmental Microbiology · doi:10.1128/aem.42.5.843-849.1981 · Cited by 20
Bacteriolytic Activity of Seminalplasmin
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Does polymyxin B nonapeptide increase outer membrane permeability in antibiotic supersensitive enterobacterial mutants?
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Authors: Vaara, M.
Affiliations: University of Helsinki (FI)
Corresponding author: Vaara, M
ORCID: Vaara, M
Venue: Microbiological Reviews
Publisher: American Society for Microbiology
Published: 1992-09
Volume: 56
Issue: 3
Pages: 395-411
ISSN: 0146-0749 (ISSN-L)
DOI: 10.1128/mr.56.3.395-411.1992
PMC: PMC372877
OpenAlex: W1895129045
Cited by: 1,879
References: 229
Citations by year: 2026: 33 · 2025: 73 · 2024: 48 · 2023: 70 · 2022: 89 · 2021: 104 · 2020: 75 · 2019: 99 · 2018: 75 · 2017: 91 · 2016: 91 · 2015: 72 · 2014: 77 · 2013: 79 · 2012: 77
FWCI: 16.64
Type: journal article
Language: en
Open access: diamond
doi.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Microbiological Reviews (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Antimicrobial agents and applications
Keywords: outer membrane permeabilization, Gram-negative bacterial outer membrane, lipopolysaccharide, cationic polymers, cationic antimicrobial peptides, polymyxins, magainin, cecropin, defensins, bactenecin, bactericidal/permeability-increasing protein, aminoglycosides, chelating agents, EDTA, antibiotic resistance, antibacterial agents
MeSH terms: Amino Acid Sequence, Anti-Bacterial Agents, Bacterial Outer Membrane Proteins, Cell Membrane Permeability, Drug Resistance, Microbial, Gram-Negative Bacteria, Lipopolysaccharides, Molecular Sequence Data

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Agents that increase the permeability of the outer membrane

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