title: Paralytic peptide: an insect cytokine that mediates innate immunity.
abstract: Host animals combat invading pathogens by activating various immune responses. Modulation of the immune pathways by cytokines is critical for efficient pathogen elimination. Insects and mammals possess common innate immune systems, and individual immune pathways have been intensively studied over the last two decades. Relatively less attention, however, has been focused on the functions of cytokines in insect innate immunity. Here, we summarize our recent findings from studies of the insect cytokine, paralytic peptide, in the silkworm Bombyx mori. The content of this report was presented at the First Asian Invertebrate Immunity Symposium. Acute activation of paralytic peptide occurs via proteolysis after stimulation with the cell wall components of pathogens, leading to the induction of a wide range of cellular and humoral immune responses. The pathogenic bacterium Serratia marcescens suppresses paralytic peptide-dependent immune activation, which impairs host resistance. Studies of insect cytokines will broaden our understanding of the basic mechanisms underlying the interaction between host innate immunity and pathogenic agents.
authors.affiliation: Department of Biological Sciences, Graduate School of Science, University of Tokyo, Tokyo, Japan.
authors.forename: Kenichi
authors.initials: K
authors.lastname: Ishii
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Hamamoto
authors.forename: Kazuhisa
authors.initials: K
authors.lastname: Sekimizu
mesh_terms: D000818:Animals; D012831:Bombyx / Q000276:immunology* / Q000382:microbiology; D016207:Cytokines / Q000276:immunology / Q000378:metabolism; D056724:Immunity, Humoral; D007113:Immunity, Innate / Q000276:immunology; D009479:Neuropeptides / Q000276:immunology* / Q000378:metabolism; D012706:Serratia marcescens / Q000276:immunology
chemical_list: D016207:Cytokines; D009479:Neuropeptides; C121924:paralytic peptide, insect
keywords: bacterial infection; insect cytokine; metalloprotease; nitric oxide; silkworm