Publications
1995
Briand J P, Guichard G, Dumortier H, Muller S
Retro-inverso peptidomimetics as new immunological probes. Validation and application to the detection of antibodies in rheumatic diseases Journal Article
In: The Journal of Biological Chemistry, vol. 270, no. 35, pp. 20686–20691, 1995, ISSN: 0021-9258.
Abstract | Links | BibTeX | Tags: Amino Acid Sequence, Animals, Antibodies, Autoantibodies, Autoimmune Diseases, Dumortier, Enzyme-Linked Immunosorbent Assay, Humans, I2CT, Immunoassay, Lupus Erythematosus, Mice, Molecular Sequence Data, Monoclonal, Peptide Fragments, Peptides, Rheumatic Diseases, Stereoisomerism, Structure-Activity Relationship, Systemic, Team-Dumortier
@article{briand_retro-inverso_1995,
title = {Retro-inverso peptidomimetics as new immunological probes. Validation and application to the detection of antibodies in rheumatic diseases},
author = {J P Briand and G Guichard and H Dumortier and S Muller},
doi = {10.1074/jbc.270.35.20686},
issn = {0021-9258},
year = {1995},
date = {1995-09-01},
journal = {The Journal of Biological Chemistry},
volume = {270},
number = {35},
pages = {20686--20691},
abstract = {Retro-inverso peptides which contain NH-CO bonds instead of CO-NH peptide bonds are much more resistant to proteolysis than L-peptides. Moreover, they have been shown recently to be able to mimic natural L-peptides with respect to poly- and monoclonal antibodies (Guichard, G., Benkirane, N., Zeder-Lutz, G., Van Regenmortel, M. H. V., Briand, J. P., and Muller, S. (1994b) Proc. Natl. Acad. Sci. U.S.A. 91, 9765-9769). We have further tested the capacity of retro-inverso peptidomimetics to serve as possible targets for antibodies produced by lupus mice and by patients with rheumatic autoimmune diseases. Several retro-inverso peptides corresponding to sequences known to be recognized by autoantibodies were synthesized, namely peptides 28-45 and 130-135 of H3, 277-291 of the Ro/SSA 52-kDa protein, and 304-324 of the Ro/SSA 60-kDa protein, and tested with autoimmune sera by enzyme-linked immunosorbent assay. We have found that retro-inverso peptides are recognized as well as or even better than natural peptides by antibodies from autoimmune patients and lupus mice. This new approach may lead to important progress in the future development of immunodiagnostic assays, particularly in the case of diseases characterized by inflammatory reactions in the course of which the level of degradative enzymes is increased.},
keywords = {Amino Acid Sequence, Animals, Antibodies, Autoantibodies, Autoimmune Diseases, Dumortier, Enzyme-Linked Immunosorbent Assay, Humans, I2CT, Immunoassay, Lupus Erythematosus, Mice, Molecular Sequence Data, Monoclonal, Peptide Fragments, Peptides, Rheumatic Diseases, Stereoisomerism, Structure-Activity Relationship, Systemic, Team-Dumortier},
pubstate = {published},
tppubtype = {article}
}
Lowenberger C, Bulet Philippe, Charlet Maurice, Hetru Charles, Hodgeman B, Christensen B M, Hoffmann Jules A
Insect immunity: isolation of three novel inducible antibacterial defensins from the vector mosquito, Aedes aegypti Journal Article
In: Insect Biochem. Mol. Biol., vol. 25, no. 7, pp. 867–873, 1995, ISSN: 0965-1748.
Abstract | BibTeX | Tags: Aedes, Amino Acid, Animals, Anti-Bacterial Agents, Blood Proteins, Defensins, Escherichia coli, Gram-Negative Bacteria, Gram-Positive Bacteria, hoffmann, Immunity, Insect Vectors, M3i, Micrococcus luteus, Sequence Homology, Stereoisomerism
@article{lowenberger_insect_1995,
title = {Insect immunity: isolation of three novel inducible antibacterial defensins from the vector mosquito, Aedes aegypti},
author = {C Lowenberger and Philippe Bulet and Maurice Charlet and Charles Hetru and B Hodgeman and B M Christensen and Jules A Hoffmann},
issn = {0965-1748},
year = {1995},
date = {1995-07-01},
journal = {Insect Biochem. Mol. Biol.},
volume = {25},
number = {7},
pages = {867--873},
abstract = {The injection of Escherichia coli and Micrococcus luteus into the hemocoel of Aedes aegypti induces a potent antibacterial activity in the hemolymph. We have purified and fully characterized three 40-residue antibacterial peptides from the hemolymph of bacteria-challenged mosquitoes that are absent in naive mosquitoes. The peptides are potently active against Gram-positive bacteria and against one of the Gram-negative bacteria that were tested. The amino acid sequences clearly show that the three peptides are novel isoforms of the insect defensin family of antibacterial peptides. They differ from each other by one or two amino acid residues. We present here the complete amino acid sequences of the three isoforms and the activity spectrum of the predominant Aedes defensin.},
keywords = {Aedes, Amino Acid, Animals, Anti-Bacterial Agents, Blood Proteins, Defensins, Escherichia coli, Gram-Negative Bacteria, Gram-Positive Bacteria, hoffmann, Immunity, Insect Vectors, M3i, Micrococcus luteus, Sequence Homology, Stereoisomerism},
pubstate = {published},
tppubtype = {article}
}