Increased stability upon heptamerization of the pore-forming toxin aerolysin (1999)
Lesieur, C., Frutiger, S., Hughes, G., Kellner, R., Pattus, F., Van Der Goot, F. G.
Aerolysin is a bacterial pore-forming toxin that is secreted as an inactive precursor, which is then processed at its COOH terminus and finally forms a circular heptameric ring which inserts into...
Moniatte, M., Van Der Goot, F. G., Buckley, J. T., Pattus, F., Van Dorsselaer, A.
Aerolysin, a virulence factor secreted by Aeromonas hydrophila, is representative of a group of beta-sheet toxins that must form stable homooligomers in order to be able to insert into biological...
Protonation of histidine-132 promotes oligomerization of the channel-forming toxin aerolysin (1995)
Buckley, J. T., Wilmsen, H. U., Lesieur, C., Schulze, A., Pattus, F., Parker, M. W., ...
Aerolysin is a bacterial toxin that binds to a receptor on eukaryotic cells and oligomerizes to form stable, SDS-resistant, noncovalent oligomers that insert into the plasma membrane and produce...
All in the family: the toxic activity of pore-forming colicins (1994)
Lakey, J.H., Van Der Goot, F. G., Pattus, F.
Colicins are unusual bacterial toxins because they are directed against close relatives of the producing strain. They kill their targets in one of three distinct ways; via a ribonuclease or...
The cytolytic toxin aerolysin: from the soluble form to the transmembrane channel (1994)
Van Der Goot, F. G., Pattus, F., Parker, M., Buckley, J. T.
Aerolysin is a cytolytic toxin which forms channels in the plasma membranes of eucaryotic cells. The protein is secreted by Aeromonas hydrophila as an inactive protoxin. Its stability and water...
Modèle d'étude de l'insertion des protéines membranaires (1993)
La colicine A produite par Citrobacter freundii et l'aérolysine produite par Aeromonas hydrophila sont deux protéines bien représentatives de classes très différentes de protéines formatrices...
Oligomerization of the channel-forming toxin aerolysin precedes insertion into lipid bilayers (1993)
Van Der Goot, F. G., Pattus, F., Wong, K. R., Buckley, J. T.
Oligomerization is a necessary step in channel formation by the bacterial toxin aerolysin. We have identified a region of aerolysin containing two tryptophans which influence the ability of the...
Van Der Goot, F. G., Didat, N., Pattus, F., Dowhan, W., Letellier, L.
Colicins A and N are pore-forming bacterial toxins that kill Escherichia coli cells. Their mode of action involves three steps; binding to specific receptors located in the outer membrane,...
Dimerization stabilizes the pore-forming toxin aerolysin in solution. (1993)
Van Der Goot, F.G., Ausio, J, Wong, K.R., Pattus, F, Buckley, J.T.
pH-dependent stability and membrane interaction of the pore-forming domain of colicin A (1993)
Muga, A., Gonzalez-Manas, J. M., Lakey, J. H., Pattus, F., Surewicz, W. K.
Thermal stability of the pore-forming domain of colicin A was studied by high sensitivity differential scanning calorimetry and circular dichroism spectroscopy. In the pH range between 8 and 5, the...
The membrane insertion of colicins (1992)
Lakey, J. H., González-Mañas, J. M., Van Der Goot, F. G., Pattus, F.
Pore-forming toxins, such as colicin A, are water-soluble proteins that insert into lipid bilayers. The water-soluble structure of Colicin A is known at a high resolution and this review describes...
Van Der Goot, F. G., Lakey, J., Pattus, F., Kay, C. M., Sorokine, O., Van Dorsselaer, A., ...
The channel-forming protein aerolysin is secreted as a protoxin which can be activated by proteolytic removal of a C-terminal peptide. The activation and subsequent oligomerization of aerolysin were...
Leippe, M., Tannich, E., Nickel, R., Pattus, F., Horstmann, R. D., ...
A pore-forming peptide is implicated in the potent cytolytic activity of pathogenic Entamoeba histolytica. Using NH2-terminal sequence information of this peptide, the corresponding cDNA was...
A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A (1991)
Van Der Goot, F. G., Gonzalez-Manas, J. M., Lakey, J. H., Pattus, F.
The 'molten' globular conformation of a protein is compact with a native secondary structure but a poorly defined tertiary structure. Molten globular states are intermediates in protein folding and...
Interaction of plasma apolipoproteins with lipid monolayers (1979)
Jackson, R.L., Pattus, F., Demel, R.A.
The monolayer technique has been used to study the interaction of lipids with plasma apolipoproteins. Apolipoprotein C-II and C-III from human very low density lipoproteins, apolipoprotein A-I from...
Jeanteur, D, Schirmer, T, Fourel, D, Simonet, V, Rummel, G, Widmer, C, ...
A strain of Escherichia coli, selected on the basis of its resistance to colicin N, reveals distinct structural and functional alterations in unspecific OmpF porin. A single mutation [Gly-119-->Asp...
Baty, D, Knibiehler, M, Verheij, H, Pattus, F, Shire, D, Bernadac, A, ...
A large number of mutants introducing point mutations and deletions into the COOH-terminal domain of colicin A have been constructed by using site-directed mutagenesis. The COOH-terminal domain...
Three-dimensional reconstruction of maltoporin from electron microscopy and image processing.
Lepault, J, Dargent, B, Tichelaar, W, Rosenbusch, J P, Leonard, K, Pattus, F
Two dimensional crystals of maltoporin (or phage lambda receptor) were obtained by reconstitution of purified maltoporin trimers and Escherichia coli phospholipids by detergent dialysis. Two...
pH-dependent membrane fusion is promoted by various colicins.
Pattus, F, Cavard, D, Crozel, V, Baty, D, Adrian, M, Lazdunski, C
The ability of colicin A, a bacteriocin produced by some Enterobacteriaceae, to fuse phospholipid vesicles at acidic pH, was demonstrated by electron microscopy and resonance energy transfer. The...
Isolation, molecular and functional properties of the C-terminal domain of colicin A.
Martinez, M C, Lazdunski, C, Pattus, F
Partial proteolytic digestion of colicin A with bromelain allowed the isolation of a 20-kd fragment. This fragment has been purified to homogeneity and its molecular properties have been studied. The...
The aerolysin membrane channel is formed by heptamerization of the monomer.
Wilmsen, H U, Leonard, K R, Tichelaar, W, Buckley, J T, Pattus, F
The cytolytic toxin aerolysin has been found to form heptameric oligomers by SDS-PAGE electrophoresis, STEM mass measurements of single oligomers and image analysis of two-dimensional membrane...
Primary and secondary structure of the pore-forming peptide of pathogenic Entamoeba histolytica.
Leippe, M, Tannich, E, Nickel, R, Pattus, F, Horstmann, R D, ...
A pore-forming peptide is implicated in the potent cytolytic activity of pathogenic Entamoeba histolytica. Using NH2-terminal sequence information of this peptide, the corresponding cDNA was...
Dargent, B, Hofmann, W, Pattus, F, Rosenbusch, J P
Phosphoporin, an Escherichia coli outer membrane-spanning protein re-incorporated in phospholipid planar bilayers generates aqueous channels similar to those of matrix porin. One phosphoporin trimer...
Jeanteur, D, Schirmer, T, Fourel, D, Simonet, V, Rummel, G, Widmer, C, ...
A strain of Escherichia coli, selected on the basis of its resistance to colicin N, reveals distinct structural and functional alterations in unspecific OmpF porin. A single mutation [Gly-119-->Asp...
Baty, D, Knibiehler, M, Verheij, H, Pattus, F, Shire, D, Bernadac, A, ...
A large number of mutants introducing point mutations and deletions into the COOH-terminal domain of colicin A have been constructed by using site-directed mutagenesis. The COOH-terminal domain...
Three-dimensional reconstruction of maltoporin from electron microscopy and image processing.
Lepault, J, Dargent, B, Tichelaar, W, Rosenbusch, J P, Leonard, K, Pattus, F
Two dimensional crystals of maltoporin (or phage lambda receptor) were obtained by reconstitution of purified maltoporin trimers and Escherichia coli phospholipids by detergent dialysis. Two...
pH-dependent membrane fusion is promoted by various colicins.
Pattus, F, Cavard, D, Crozel, V, Baty, D, Adrian, M, Lazdunski, C
The ability of colicin A, a bacteriocin produced by some Enterobacteriaceae, to fuse phospholipid vesicles at acidic pH, was demonstrated by electron microscopy and resonance energy transfer. The...
Isolation, molecular and functional properties of the C-terminal domain of colicin A.
Martinez, M C, Lazdunski, C, Pattus, F
Partial proteolytic digestion of colicin A with bromelain allowed the isolation of a 20-kd fragment. This fragment has been purified to homogeneity and its molecular properties have been studied. The...
The aerolysin membrane channel is formed by heptamerization of the monomer.
Wilmsen, H U, Leonard, K R, Tichelaar, W, Buckley, J T, Pattus, F
The cytolytic toxin aerolysin has been found to form heptameric oligomers by SDS-PAGE electrophoresis, STEM mass measurements of single oligomers and image analysis of two-dimensional membrane...
Primary and secondary structure of the pore-forming peptide of pathogenic Entamoeba histolytica.
Leippe, M, Tannich, E, Nickel, R, Pattus, F, Horstmann, R D, ...
A pore-forming peptide is implicated in the potent cytolytic activity of pathogenic Entamoeba histolytica. Using NH2-terminal sequence information of this peptide, the corresponding cDNA was...
Dargent, B, Hofmann, W, Pattus, F, Rosenbusch, J P
Phosphoporin, an Escherichia coli outer membrane-spanning protein re-incorporated in phospholipid planar bilayers generates aqueous channels similar to those of matrix porin. One phosphoporin trimer...