Innate immunity in higher insects

Approaching the Asymptote? Evolution and Revolution in Immunology

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A recessive mutation, immune deficiency (imd), defines two distinct control pathways in the Drosophila host defense.

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Innate immunity of insects

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Dif, a dorsal-related gene that mediates an immune response in Drosophila

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Apidaecins: antibacterial peptides from honeybees.

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Insect immunity. Septic injury of Drosophila induces the synthesis of a potent antifungal peptide with sequence homology to plant antifungal peptides

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Antibacterial peptides from pig intestine: isolation of a mammalian cecropin.

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Embryonic origin of hemocytes and their relationship to cell death in Drosophila

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A novel inducible antibacterial peptide of Drosophila carries an O-glycosylated substitution

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Structure-activity analysis of thanatin, a 21-residue inducible insect defense peptide with sequence homology to frog skin antimicrobial peptides.

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Refined three-dimensional solution structure of insect defensin A

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Functional analysis and regulation of nuclear import of dorsal during the immune response in Drosophila.

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Expression cloning of dSR-CI, a class C macrophage-specific scavenger receptor from Drosophila melanogaster.

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Metchnikowin, a Novel Immune‐Inducible Proline‐Rich Peptide from Drosophila with Antibacterial and Antifungal Properties

Levashina, E. A., Ohresser, S., Bulet, P., Reichhart, J., Hetru, C., & Hoffmann, J. A. (1995) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1995.694_2.x · Cited by 227

κB-like Motifs Regulate the Induction of Immune Genes in Drosophila

Engström, Y., Kadalayil, L., Sun, S.-C., Samakovlis, C., Hultmark, D., & Faye, I. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1392 · Cited by 224

Proenzyme of Manduca sexta phenol oxidase: purification, activation, substrate specificity of the active enzyme, and molecular cloning.

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Novel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug Pyrrhocoris apterus

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Characterization and transcriptional profiles of a Drosophila gene encoding an insect defensin: A study in insect immunity

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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.

Kappler, C., Meister, M., Lagueux, M., Gateff, E., Hoffmann, J. A., & Reichhart, J. M. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05800.x · Cited by 158

Nucleotide sequence of the cDNA encoding the proenzyme of phenol oxidase A1 of Drosophila melanogaster.

Fujimoto, K., Okino, N., Kawabata, S., Iwanaga, S., & Ohnishi, E. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.17.7769 · Cited by 147

The Drosophila 18 wheeler is required for morphogenesis and has striking similarities to Toll

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A novel antibacterial peptide family isolated from the silkworm, Bombyx mori

Hara, S., & Yamakawa, M. (1995) · Biochemical Journal · doi:10.1042/bj3100651 · Cited by 144

Signals from the IL-1 Receptor Homolog, Toll, Can Activate an Immune Response in a Drosophila Hemocyte Cell Line

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Apidaecin-Type Peptide Antibiotics Function through a Nonporeforming Mechanism Involving Stereospecificity

Casteels, P., & Tempst, P. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1234 · Cited by 134

Cloning and expression of the gene of hemocytin, an insect humoral lectin which is homologous with the mammalian von Willebrand factor

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Purification, characterization, and cDNA cloning of an antifungal protein from the hemolymph of Sarcophaga peregrina (flesh fly) larvae

Iijima, R., Kurata, S., & Natori, S. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50307-6 · Cited by 121

Apidaecin multipeptide precursor structure: a putative mechanism for amplification of the insect antibacterial response.

Casteels-Josson, K., Capaci, T. M., Casteels, P., & Tempst, P. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05801.x · Cited by 115

The Drosophila membrane receptor Toll can function to promote cellular adhesion.

Keith, F. J., & Gay, N. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07878.x · Cited by 114

The dorsal‐related immunity factor, Dif, is a sequence‐specific trans‐activator of Drosophila Cecropin gene expression.

Petersen, U.-M., Björklund, G., Ip, Y. T., & Engström, Y. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07317.x · Cited by 108

Macrophages in Drosophila embryos and L2 cells exhibit scavenger receptor-mediated endocytosis.

Abrams, J., Lux, A., Steller, H., & Krieger, M. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.21.10375 · Cited by 102

The lysozyme locus in Drosophila melanogaster: different genes are expressed in midgut and salivary glands

Kylsten, P., Kimbrell, D. A., Daffre, S., Samakovlis, C., & Hultmark, D. (1992) · Molecular and General Genetics MGG · doi:10.1007/bf00266235 · Cited by 96

Biodiversity of apidaecin-type peptide antibiotics. Prospects of manipulating the antibacterial spectrum and combating acquired resistance

Casteels, P., Romagnolo, J., Castle, M., Casteels-Josson, K., Erdjument‐Bromage, H., & Tempst, P. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47165-7 · Cited by 93

Expression and nuclear translocation of the rel/NF-kappa B-related morphogen dorsal during the immune response of Drosophila.

Reichhart, J., Georgel, P., Meister, M. F., Lemaître, B., Kappler, C., & Hoffmann, J. A. (1993) · PubMed · Cited by 89

Insect immunity. A transgenic analysis in Drosophila defines several functional domains in the diptericin promoter.

Meister, M. F., Braun, A., Kappler, C., Reichhart, J., & Hoffmann, J. A. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06941.x · Cited by 85

A conserved signal transduction pathway regulating the activity of the rel-like proteins dorsal and NF-kappa B.

Wasserman, S. A. (1993) · Molecular Biology of the Cell · doi:10.1091/mbc.4.8.767 · Cited by 85

Characterization of a Bombyx mori cDNA encoding a novel member of the attacin family of insect antibacterial proteins

Sugiyama, M., Kuniyoshi, H., Kotani, E., Taniai, K., Kadono‐Okuda, K., Kato, Y., Yamamoto, M., Shimabukuro, M., Chowdhury, S., Xu, J., et al. (1995) · Insect Biochemistry and Molecular Biology · doi:10.1016/0965-1748(94)00080-2 · Cited by 79

Drosophilaimmunity. A sequence homologous to mammalian interferon consensus response element enhances the activity of the diptericin promoter

Georgel, P., Kappler, C., Langley, E., Groß, I., Nicolas, E., Reichhart, J., & Hoffmann, J. A. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.7.1140 · Cited by 47

Ability of cecropin B to penetrate the enterobacterial outer membrane

Vaara, M., & Vaara, T. (1994) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.38.10.2498 · Cited by 42

Cell-penetrating peptides

Lindgren, M., Hällbrink, M., Prochiantz, A., & Langel, Ü. (2000) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(00)01447-4 · Cited by 803

Penaeidins, a New Family of Antimicrobial Peptides Isolated from the Shrimp Penaeus vannamei (Decapoda)

Destoumieux, D., Bulet, P., Loew, D., Van Dorsselaer, A., Rodriguez, J., & Bachère, E. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.45.28398 · Cited by 441

Functional analysis of regulatory sequences controllingPR‐1 gene expression in Arabidopsis

Lebel, E., Heifetz, P., Thorne, L., Uknes, S., Ryals, J., & Ward, E. (1998) · The Plant Journal · doi:10.1046/j.1365-313x.1998.00288.x · Cited by 356

ECSIT is an evolutionarily conserved intermediate in the Toll/IL-1 signal transduction pathway

Kopp, E., Medzhitov, R., Carothers, J., Xiao, C., Douglas, I., Janeway, C. A., & Ghosh, S. (1999) · Genes & Development · doi:10.1101/gad.13.16.2059 · Cited by 334

A Lipopolysaccharide- and β-1,3-Glucan-binding Protein from Hemocytes of the Freshwater Crayfish Pacifastacus leniusculus

Lee, S. Y., Wang, R., & Söderhäll, K. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.2.1337 · Cited by 294