Intranet
Acces
Contact
Publications
2005 |
Lescoute, A; Leontis, N B; Massire, C; Westhof, E Recurrent structural RNA motifs, Isostericity Matrices and sequence alignments Article de journal Nucleic Acids Res, 33 (8), p. 2395-2409, 2005, ISBN: 15860776, (1362-4962 Journal Article). Résumé | Liens | BibTeX | Étiquettes: Molecular Nucleic Acid Conformation RNA, Non-U.S. Gov't Research Support, Nucleic Acid, P.H.S. *Sequence Alignment Sequence Analysis, Ribosomal/*chemistry Research Support, RNA/*methods Sequence Homology, U.S. Gov't, Unité ARN, WESTHOF Base Pairing Models @article{, title = {Recurrent structural RNA motifs, Isostericity Matrices and sequence alignments}, author = {A Lescoute and N B Leontis and C Massire and E Westhof}, url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15860776}, isbn = {15860776}, year = {2005}, date = {2005-01-01}, journal = {Nucleic Acids Res}, volume = {33}, number = {8}, pages = {2395-2409}, abstract = {The occurrences of two recurrent motifs in ribosomal RNA sequences, the Kink-turn and the C-loop, are examined in crystal structures and systematically compared with sequence alignments of rRNAs from the three kingdoms of life in order to identify the range of the structural and sequence variations. Isostericity Matrices are used to analyze structurally the sequence variations of the characteristic non-Watson-Crick base pairs for each motif. We show that Isostericity Matrices for non-Watson-Crick base pairs provide important tools for deriving the sequence signatures of recurrent motifs, for scoring and refining sequence alignments, and for determining whether motifs are conserved throughout evolution. The systematic use of Isostericity Matrices identifies the positions of the insertion or deletion of one or more nucleotides relative to the structurally characterized examples of motifs and, most importantly, specifies whether these changes result in new motifs. Thus, comparative analysis coupled with Isostericity Matrices allows one to produce and refine structural sequence alignments. The analysis, based on both sequence and structure, permits therefore the evaluation of the conservation of motifs across phylogeny and the derivation of rules of equivalence between structural motifs. The conservations observed in Isostericity Matrices form a predictive basis for identifying motifs in sequences.}, note = {1362-4962 Journal Article}, keywords = {Molecular Nucleic Acid Conformation RNA, Non-U.S. Gov't Research Support, Nucleic Acid, P.H.S. *Sequence Alignment Sequence Analysis, Ribosomal/*chemistry Research Support, RNA/*methods Sequence Homology, U.S. Gov't, Unité ARN, WESTHOF Base Pairing Models}, pubstate = {published}, tppubtype = {article} } The occurrences of two recurrent motifs in ribosomal RNA sequences, the Kink-turn and the C-loop, are examined in crystal structures and systematically compared with sequence alignments of rRNAs from the three kingdoms of life in order to identify the range of the structural and sequence variations. Isostericity Matrices are used to analyze structurally the sequence variations of the characteristic non-Watson-Crick base pairs for each motif. We show that Isostericity Matrices for non-Watson-Crick base pairs provide important tools for deriving the sequence signatures of recurrent motifs, for scoring and refining sequence alignments, and for determining whether motifs are conserved throughout evolution. The systematic use of Isostericity Matrices identifies the positions of the insertion or deletion of one or more nucleotides relative to the structurally characterized examples of motifs and, most importantly, specifies whether these changes result in new motifs. Thus, comparative analysis coupled with Isostericity Matrices allows one to produce and refine structural sequence alignments. The analysis, based on both sequence and structure, permits therefore the evaluation of the conservation of motifs across phylogeny and the derivation of rules of equivalence between structural motifs. The conservations observed in Isostericity Matrices form a predictive basis for identifying motifs in sequences. |
1995 |
Lemaitre, Bruno; Kromer-Metzger, E; Michaut, Lydia; Nicolas, E; Meister, Marie; Georgel, Philippe; Reichhart, Jean-Marc; Hoffmann, Jules A A recessive mutation, immune deficiency (imd), defines two distinct control pathways in the Drosophila host defense Article de journal Proc. Natl. Acad. Sci. U.S.A., 92 (21), p. 9465–9469, 1995, ISSN: 0027-8424. Résumé | BibTeX | Étiquettes: Animals, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Bacterial Infections, Base Sequence, Gene Expression Regulation, Genes, Glycopeptides, hoffmann, Insect, Insect Hormones, Insect Proteins, M3i, Male, Mutation, Mycoses, Nucleic Acid, Peptides, Protein Binding, Recessive, Regulatory Sequences, reichhart, Reporter, Survival Analysis @article{lemaitre_recessive_1995, title = {A recessive mutation, immune deficiency (imd), defines two distinct control pathways in the Drosophila host defense}, author = {Bruno Lemaitre and E Kromer-Metzger and Lydia Michaut and E Nicolas and Marie Meister and Philippe Georgel and Jean-Marc Reichhart and Jules A Hoffmann}, issn = {0027-8424}, year = {1995}, date = {1995-10-01}, journal = {Proc. Natl. Acad. Sci. U.S.A.}, volume = {92}, number = {21}, pages = {9465--9469}, abstract = {In this paper we report a recessive mutation, immune deficiency (imd), that impairs the inducibility of all genes encoding antibacterial peptides during the immune response of Drosophila. When challenged with bacteria, flies carrying this mutation show a lower survival rate than wild-type flies. We also report that, in contrast to the antibacterial peptides, the antifungal peptide drosomycin remains inducible in a homozygous imd mutant background. These results point to the existence of two different pathways leading to the expression of two types of target genes, encoding either the antibacterial peptides or the antifungal peptide drosomycin.}, keywords = {Animals, Anti-Bacterial Agents, Antimicrobial Cationic Peptides, Bacterial Infections, Base Sequence, Gene Expression Regulation, Genes, Glycopeptides, hoffmann, Insect, Insect Hormones, Insect Proteins, M3i, Male, Mutation, Mycoses, Nucleic Acid, Peptides, Protein Binding, Recessive, Regulatory Sequences, reichhart, Reporter, Survival Analysis}, pubstate = {published}, tppubtype = {article} } In this paper we report a recessive mutation, immune deficiency (imd), that impairs the inducibility of all genes encoding antibacterial peptides during the immune response of Drosophila. When challenged with bacteria, flies carrying this mutation show a lower survival rate than wild-type flies. We also report that, in contrast to the antibacterial peptides, the antifungal peptide drosomycin remains inducible in a homozygous imd mutant background. These results point to the existence of two different pathways leading to the expression of two types of target genes, encoding either the antibacterial peptides or the antifungal peptide drosomycin. |
1994 |
Meister, Marie; Braun, A; Kappler, Christine; Reichhart, Jean-Marc; Hoffmann, Jules A Insect immunity. A transgenic analysis in Drosophila defines several functional domains in the diptericin promoter Article de journal EMBO J., 13 (24), p. 5958–5966, 1994, ISSN: 0261-4189. Résumé | BibTeX | Étiquettes: Animals, Anti-Infective Agents, Base Sequence, beta-Galactosidase, DNA Mutational Analysis, Female, Gene Expression Regulation, Genetic, Genetically Modified, Germ Cells, hoffmann, Insect Hormones, Insect Proteins, M3i, Male, Models, Nucleic Acid, Promoter Regions, Recombinant Fusion Proteins, reichhart, Repetitive Sequences, Transformation @article{meister_insect_1994, title = {Insect immunity. A transgenic analysis in Drosophila defines several functional domains in the diptericin promoter}, author = {Marie Meister and A Braun and Christine Kappler and Jean-Marc Reichhart and Jules A Hoffmann}, issn = {0261-4189}, year = {1994}, date = {1994-12-01}, journal = {EMBO J.}, volume = {13}, number = {24}, pages = {5958--5966}, abstract = {Diptericins are antibacterial polypeptides which are strongly induced in the fat body and blood cells of dipteran insects in response to septic injury. The promoter of the single-copy, intronless diptericin gene of Drosophila contains several nucleotide sequences homologous to mammalian cis-regulatory motifs involved in the control of acute phase response genes. Extending our previous studies on the expression of the diptericin gene, we now report a quantitative analysis of the contribution of various putative regulatory elements to the bacterial inducibility of this gene, based on the generation of 60 transgenic fly lines carrying different elements fused to a reporter gene. Our data definitively identify two Kappa B-related motifs in the proximal promoter as the sites conferring inducibility and tissue-specific expression to the diptericin gene. These motifs alone, however, mediate only minimal levels of expression. Additional proximal regulatory elements are necessary to attain some 20% of the full response and we suspect a role for sequences homologous to mammalian IL6 response elements and interferon-gamma responsive sites in this up-regulation. The transgenic experiments also reveal the existence of a distal regulatory element located upstream of -0.6 kb which increases the level of expression by a factor of five.}, keywords = {Animals, Anti-Infective Agents, Base Sequence, beta-Galactosidase, DNA Mutational Analysis, Female, Gene Expression Regulation, Genetic, Genetically Modified, Germ Cells, hoffmann, Insect Hormones, Insect Proteins, M3i, Male, Models, Nucleic Acid, Promoter Regions, Recombinant Fusion Proteins, reichhart, Repetitive Sequences, Transformation}, pubstate = {published}, tppubtype = {article} } Diptericins are antibacterial polypeptides which are strongly induced in the fat body and blood cells of dipteran insects in response to septic injury. The promoter of the single-copy, intronless diptericin gene of Drosophila contains several nucleotide sequences homologous to mammalian cis-regulatory motifs involved in the control of acute phase response genes. Extending our previous studies on the expression of the diptericin gene, we now report a quantitative analysis of the contribution of various putative regulatory elements to the bacterial inducibility of this gene, based on the generation of 60 transgenic fly lines carrying different elements fused to a reporter gene. Our data definitively identify two Kappa B-related motifs in the proximal promoter as the sites conferring inducibility and tissue-specific expression to the diptericin gene. These motifs alone, however, mediate only minimal levels of expression. Additional proximal regulatory elements are necessary to attain some 20% of the full response and we suspect a role for sequences homologous to mammalian IL6 response elements and interferon-gamma responsive sites in this up-regulation. The transgenic experiments also reveal the existence of a distal regulatory element located upstream of -0.6 kb which increases the level of expression by a factor of five. |
Dimarcq, Jean-Luc; Hoffmann, Danièle; Meister, Marie; Bulet, Philippe; Lanot, R; Reichhart, Jean-Marc; Hoffmann, Jules A Characterization and transcriptional profiles of a Drosophila gene encoding an insect defensin. A study in insect immunity Article de journal Eur. J. Biochem., 221 (1), p. 201–209, 1994, ISSN: 0014-2956. Résumé | BibTeX | Étiquettes: Animals, Base Sequence, Blood Proteins, Chromosome Mapping, Cloning, Complementary, Defensins, DNA, Gene Expression, Genetic, Gram-Positive Bacteria, hoffmann, Larva, M3i, Molecular, Molecular Structure, Nucleic Acid, Protein Precursors, Regulatory Sequences, reichhart, Transcription @article{dimarcq_characterization_1994, title = {Characterization and transcriptional profiles of a Drosophila gene encoding an insect defensin. A study in insect immunity}, author = {Jean-Luc Dimarcq and Danièle Hoffmann and Marie Meister and Philippe Bulet and R Lanot and Jean-Marc Reichhart and Jules A Hoffmann}, issn = {0014-2956}, year = {1994}, date = {1994-04-01}, journal = {Eur. J. Biochem.}, volume = {221}, number = {1}, pages = {201--209}, abstract = {Insect defensins are a family of 4-kDa, cationic, inducible antibacterial peptides which bear six cysteine residues engaged in three intramolecular disulfide bridges. They owe their name to certain sequence similarities with defensins from mammalian neutrophiles and macrophages. We report the characterization of a novel defensin isoform from Drosophila and the cloning of the gene encoding a preprodefensin. The gene, which is intronless and present in a single copy/haploid genome, maps at position 46CD on the right arm of the second chromosome. The analysis of the upstream region of the gene reveals the presence of multiple putative cis-regulatory sequences similar to mammalian regulatory motifs of acute-phase-response genes. Transcriptional profiles indicate that the Drosophila defensin gene is induced by bacterial challenge with acute-phase kinetics. It is also expressed in the absence of immune challenge during metamorphosis. These and other data on the Drosophila defensin gene lead us to suggest that insect and mammalian defensins have evolved independently.}, keywords = {Animals, Base Sequence, Blood Proteins, Chromosome Mapping, Cloning, Complementary, Defensins, DNA, Gene Expression, Genetic, Gram-Positive Bacteria, hoffmann, Larva, M3i, Molecular, Molecular Structure, Nucleic Acid, Protein Precursors, Regulatory Sequences, reichhart, Transcription}, pubstate = {published}, tppubtype = {article} } Insect defensins are a family of 4-kDa, cationic, inducible antibacterial peptides which bear six cysteine residues engaged in three intramolecular disulfide bridges. They owe their name to certain sequence similarities with defensins from mammalian neutrophiles and macrophages. We report the characterization of a novel defensin isoform from Drosophila and the cloning of the gene encoding a preprodefensin. The gene, which is intronless and present in a single copy/haploid genome, maps at position 46CD on the right arm of the second chromosome. The analysis of the upstream region of the gene reveals the presence of multiple putative cis-regulatory sequences similar to mammalian regulatory motifs of acute-phase-response genes. Transcriptional profiles indicate that the Drosophila defensin gene is induced by bacterial challenge with acute-phase kinetics. It is also expressed in the absence of immune challenge during metamorphosis. These and other data on the Drosophila defensin gene lead us to suggest that insect and mammalian defensins have evolved independently. |
1993 |
Georgel, Philippe; Meister, Marie; Kappler, Christine; Lemaitre, Bruno; Reichhart, Jean-Marc; Hoffmann, Jules A Insect immunity: the diptericin promoter contains multiple functional regulatory sequences homologous to mammalian acute-phase response elements Article de journal Biochem. Biophys. Res. Commun., 197 (2), p. 508–517, 1993, ISSN: 0006-291X. Résumé | Liens | BibTeX | Étiquettes: Acute-Phase Proteins, Animals, Anti-Infective Agents, Base Sequence, Cell Line, Deoxyribonuclease I, DNA-Binding Proteins, Genetic, hoffmann, Insect Hormones, Insect Proteins, Larva, M3i, Mammals, NF-kappa B, Nucleic Acid, Oligonucleotide Probes, Polymerase Chain Reaction, Promoter Regions, Regulatory Sequences, reichhart @article{georgel_insect_1993, title = {Insect immunity: the diptericin promoter contains multiple functional regulatory sequences homologous to mammalian acute-phase response elements}, author = {Philippe Georgel and Marie Meister and Christine Kappler and Bruno Lemaitre and Jean-Marc Reichhart and Jules A Hoffmann}, doi = {10.1006/bbrc.1993.2508}, issn = {0006-291X}, year = {1993}, date = {1993-12-01}, journal = {Biochem. Biophys. Res. Commun.}, volume = {197}, number = {2}, pages = {508--517}, abstract = {We are using the diptericin gene as a model system to study the control of expression of the genes encoding antibacterial peptides during the Drosophila immune reaction. In order to investigate the putative regulatory regions in the diptericin promoter, we performed DNaseI footprinting experiments combined with gel-shift assays in two inducible systems: the larval fat body and a tumorous Drosophila blood cell line. Our results confirm the importance of kappa B-like elements previously described in the immune response of insects and reveal for the first time the involvement of other regions containing sequences homologous to mammalian acute-phase response elements.}, keywords = {Acute-Phase Proteins, Animals, Anti-Infective Agents, Base Sequence, Cell Line, Deoxyribonuclease I, DNA-Binding Proteins, Genetic, hoffmann, Insect Hormones, Insect Proteins, Larva, M3i, Mammals, NF-kappa B, Nucleic Acid, Oligonucleotide Probes, Polymerase Chain Reaction, Promoter Regions, Regulatory Sequences, reichhart}, pubstate = {published}, tppubtype = {article} } We are using the diptericin gene as a model system to study the control of expression of the genes encoding antibacterial peptides during the Drosophila immune reaction. In order to investigate the putative regulatory regions in the diptericin promoter, we performed DNaseI footprinting experiments combined with gel-shift assays in two inducible systems: the larval fat body and a tumorous Drosophila blood cell line. Our results confirm the importance of kappa B-like elements previously described in the immune response of insects and reveal for the first time the involvement of other regions containing sequences homologous to mammalian acute-phase response elements. |
Kappler, Christine; Meister, Marie; Lagueux, Marie; Gateff, E; Hoffmann, Jules A; Reichhart, Jean-Marc Insect immunity. Two 17 bp repeats nesting a kappa B-related sequence confer inducibility to the diptericin gene and bind a polypeptide in bacteria-challenged Drosophila Article de journal EMBO J., 12 (4), p. 1561–1568, 1993, ISSN: 0261-4189. Résumé | BibTeX | Étiquettes: Animals, Anti-Bacterial Agents, Base Sequence, Cloning, Gene Expression Regulation, Genes, Genetic, Genetically Modified, hoffmann, Insect, Insect Hormones, Insect Proteins, Lipopolysaccharides, M3i, messenger, Molecular, NF-kappa B, Nucleic Acid, Oligodeoxyribonucleotides, Promoter Regions, Regulatory Sequences, reichhart, RNA, Transfection @article{kappler_insect_1993, title = {Insect immunity. Two 17 bp repeats nesting a kappa B-related sequence confer inducibility to the diptericin gene and bind a polypeptide in bacteria-challenged Drosophila}, author = {Christine Kappler and Marie Meister and Marie Lagueux and E Gateff and Jules A Hoffmann and Jean-Marc Reichhart}, issn = {0261-4189}, year = {1993}, date = {1993-04-01}, journal = {EMBO J.}, volume = {12}, number = {4}, pages = {1561--1568}, abstract = {The Drosophila diptericin gene codes for a 9 kDa antibacterial peptide and is rapidly and transiently expressed in larvae and adults after bacterial challenge. It is also induced in a tumorous Drosophila blood cell line by the addition of lipopolysaccharide (LPS). The promoter of this gene contains two 17 bp repeats located closely upstream of the TATA-box and harbouring a decameric kappa B-related sequence. This study reports that the replacement of the two 17 bp repeats by random sequences abolishes bacteria inducibility in transgenic fly lines. In transfected tumorous blood cells, the replacement of both or either of the 17 bp motifs reduces dramatically LPS inducibility, whereas multiple copies significantly increase the level of transcriptional activation by LPS challenge. A specific DNA-protein binding activity is evidenced in cytoplasmic and nuclear extracts of induced blood cells and fat body. It is absent in controls. It is proposed that induction of the diptericin gene mediated by the two 17 bp repeats occurs via a mechanism similar to that of mammalian NF-kappa B.}, keywords = {Animals, Anti-Bacterial Agents, Base Sequence, Cloning, Gene Expression Regulation, Genes, Genetic, Genetically Modified, hoffmann, Insect, Insect Hormones, Insect Proteins, Lipopolysaccharides, M3i, messenger, Molecular, NF-kappa B, Nucleic Acid, Oligodeoxyribonucleotides, Promoter Regions, Regulatory Sequences, reichhart, RNA, Transfection}, pubstate = {published}, tppubtype = {article} } The Drosophila diptericin gene codes for a 9 kDa antibacterial peptide and is rapidly and transiently expressed in larvae and adults after bacterial challenge. It is also induced in a tumorous Drosophila blood cell line by the addition of lipopolysaccharide (LPS). The promoter of this gene contains two 17 bp repeats located closely upstream of the TATA-box and harbouring a decameric kappa B-related sequence. This study reports that the replacement of the two 17 bp repeats by random sequences abolishes bacteria inducibility in transgenic fly lines. In transfected tumorous blood cells, the replacement of both or either of the 17 bp motifs reduces dramatically LPS inducibility, whereas multiple copies significantly increase the level of transcriptional activation by LPS challenge. A specific DNA-protein binding activity is evidenced in cytoplasmic and nuclear extracts of induced blood cells and fat body. It is absent in controls. It is proposed that induction of the diptericin gene mediated by the two 17 bp repeats occurs via a mechanism similar to that of mammalian NF-kappa B. |
1990 |
Hoffmann, Jules A; Hoffmann, Danièle The inducible antibacterial peptides of dipteran insects Article de journal Res. Immunol., 141 (9), p. 910–918, 1990, ISSN: 0923-2494. BibTeX | Étiquettes: Animals, Antimicrobial Cationic Peptides, Defensins, Diptera, Gene Expression Regulation, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, Nucleic Acid, Proteins, Sequence Homology, Transcription @article{hoffmann_inducible_1990, title = {The inducible antibacterial peptides of dipteran insects}, author = {Jules A Hoffmann and Danièle Hoffmann}, issn = {0923-2494}, year = {1990}, date = {1990-12-01}, journal = {Res. Immunol.}, volume = {141}, number = {9}, pages = {910--918}, keywords = {Animals, Antimicrobial Cationic Peptides, Defensins, Diptera, Gene Expression Regulation, Genetic, hoffmann, Insect Hormones, Insect Proteins, M3i, Nucleic Acid, Proteins, Sequence Homology, Transcription}, pubstate = {published}, tppubtype = {article} } |
Lagueux, Marie; Lwoff, L; Meister, Marie; Goltzené, F; Hoffmann, Jules A cDNAs from neurosecretory cells of brains of Locusta migratoria (Insecta, Orthoptera) encoding a novel member of the superfamily of insulins Article de journal Eur. J. Biochem., 187 (1), p. 249–254, 1990, ISSN: 0014-2956. Résumé | BibTeX | Étiquettes: Animals, Base Sequence, DNA, Genes, Grasshoppers, hoffmann, Humans, Insulin, M3i, Multigene Family, Nervous System, Neuropeptides, Neurosecretory Systems, Nucleic Acid, Nucleic Acid Hybridization, Oligonucleotide Probes, RNA, Sequence Homology @article{lagueux_cdnas_1990, title = {cDNAs from neurosecretory cells of brains of Locusta migratoria (Insecta, Orthoptera) encoding a novel member of the superfamily of insulins}, author = {Marie Lagueux and L Lwoff and Marie Meister and F Goltzené and Jules A Hoffmann}, issn = {0014-2956}, year = {1990}, date = {1990-01-01}, journal = {Eur. J. Biochem.}, volume = {187}, number = {1}, pages = {249--254}, abstract = {From neurohaemal lobes of corpora cardiaca of Locusta migratoria a 5-kDa peptide has been isolated and its sequence established [see the accompanying paper, by Hietter et al. (1990) Eur. J. Biochem. 187, 241-247]. We have designed oligonucleotide probes from the peptide sequence of this molecule and screened a library prepared from mRNA of the neurosecretory cell region of the brain of this insect. Several positive cDNAs were isolated, the combined nucleotide sequences of which predict a large precursor of 145 residues (15770 Da) containing the newly isolated 5-kDa peptide. The peptide is flanked by regions homologous to the A and B chains of the superfamily of insulins. The overall organization of the precursor is as follows: signal peptide/domain homologous to the B chain of insulins/C (connecting)-peptide (corresponding to the newly isolated 5-kDa peptide)/domain homologous to the A chain of insulins. The numbers and relative positions of the cysteines of the Locusta peptide are equivalent to those of the other members of the insulin superfamily and most of the hydrophobic core residues are conserved.}, keywords = {Animals, Base Sequence, DNA, Genes, Grasshoppers, hoffmann, Humans, Insulin, M3i, Multigene Family, Nervous System, Neuropeptides, Neurosecretory Systems, Nucleic Acid, Nucleic Acid Hybridization, Oligonucleotide Probes, RNA, Sequence Homology}, pubstate = {published}, tppubtype = {article} } From neurohaemal lobes of corpora cardiaca of Locusta migratoria a 5-kDa peptide has been isolated and its sequence established [see the accompanying paper, by Hietter et al. (1990) Eur. J. Biochem. 187, 241-247]. We have designed oligonucleotide probes from the peptide sequence of this molecule and screened a library prepared from mRNA of the neurosecretory cell region of the brain of this insect. Several positive cDNAs were isolated, the combined nucleotide sequences of which predict a large precursor of 145 residues (15770 Da) containing the newly isolated 5-kDa peptide. The peptide is flanked by regions homologous to the A and B chains of the superfamily of insulins. The overall organization of the precursor is as follows: signal peptide/domain homologous to the B chain of insulins/C (connecting)-peptide (corresponding to the newly isolated 5-kDa peptide)/domain homologous to the A chain of insulins. The numbers and relative positions of the cysteines of the Locusta peptide are equivalent to those of the other members of the insulin superfamily and most of the hydrophobic core residues are conserved. |
Wicker, C; Reichhart, Jean-Marc; Hoffmann, Danièle; Hultmark, D; Samakovlis, C; Hoffmann, Jules A Insect immunity. Characterization of a Drosophila cDNA encoding a novel member of the diptericin family of immune peptides Article de journal J. Biol. Chem., 265 (36), p. 22493–22498, 1990, ISSN: 0021-9258. Résumé | BibTeX | Étiquettes: Animals, Anti-Bacterial Agents, Base Sequence, Cloning, Diptera, DNA, Escherichia coli, hoffmann, Insect Hormones, Insect Proteins, M3i, Molecular, Multigene Family, Nucleic Acid, Oligonucleotide Probes, reichhart, Sequence Homology @article{wicker_insect_1990, title = {Insect immunity. Characterization of a Drosophila cDNA encoding a novel member of the diptericin family of immune peptides}, author = {C Wicker and Jean-Marc Reichhart and Danièle Hoffmann and D Hultmark and C Samakovlis and Jules A Hoffmann}, issn = {0021-9258}, year = {1990}, date = {1990-01-01}, journal = {J. Biol. Chem.}, volume = {265}, number = {36}, pages = {22493--22498}, abstract = {Drosophila shows an immune response when challenged by injection of low doses of bacteria. To date, the molecules involved in this immune reaction have remained elusive, with the exception of cecropins (4-kDa antibacterial peptides initially isolated from the moth Hyalophora cecropia) for which three closely related genes have been characterized recently. We report the molecular cloning and sequencing of a cDNA from a library of immune Drosophila which encodes a novel member of the family of diptericins (9-kDa antibacterial peptides initially isolated from the fly Phormia terranovae). Transcripts for the Drosophila diptericin are detected 2 h after injection of bacteria. They are apparently derived from a single gene mapping at position 56 A on the right arm of the second chromosome. We discuss the existence of a distant relationship between the diptericins and two other groups of anti-bacterial insect proteins, the attacins, and the sarcotoxins II.}, keywords = {Animals, Anti-Bacterial Agents, Base Sequence, Cloning, Diptera, DNA, Escherichia coli, hoffmann, Insect Hormones, Insect Proteins, M3i, Molecular, Multigene Family, Nucleic Acid, Oligonucleotide Probes, reichhart, Sequence Homology}, pubstate = {published}, tppubtype = {article} } Drosophila shows an immune response when challenged by injection of low doses of bacteria. To date, the molecules involved in this immune reaction have remained elusive, with the exception of cecropins (4-kDa antibacterial peptides initially isolated from the moth Hyalophora cecropia) for which three closely related genes have been characterized recently. We report the molecular cloning and sequencing of a cDNA from a library of immune Drosophila which encodes a novel member of the family of diptericins (9-kDa antibacterial peptides initially isolated from the fly Phormia terranovae). Transcripts for the Drosophila diptericin are detected 2 h after injection of bacteria. They are apparently derived from a single gene mapping at position 56 A on the right arm of the second chromosome. We discuss the existence of a distant relationship between the diptericins and two other groups of anti-bacterial insect proteins, the attacins, and the sarcotoxins II. |