title: Eater, a transmembrane protein mediating phagocytosis of bacterial pathogens in Drosophila.
abstract: Phagocytosis is a complex, evolutionarily conserved process that plays a central role in host defense against infection. We have identified a predicted transmembrane protein, Eater, which is involved in phagocytosis in Drosophila. Transcriptional silencing of the eater gene in a macrophage cell line led to a significant reduction in the binding and internalization of bacteria. Moreover, the N terminus of the Eater protein mediated direct microbial binding which could be inhibited with scavenger receptor ligands, acetylated, and oxidized low-density lipoprotein. In vivo, eater expression was restricted to blood cells. Flies lacking the eater gene displayed normal responses in NF-kappaB-like Toll and IMD signaling pathways but showed impaired phagocytosis and decreased survival after bacterial infection. Our results suggest that Eater is a major phagocytic receptor for a broad range of bacterial pathogens in Drosophila and provide a powerful model to address the role of phagocytosis in vivo.
authors.affiliation: Laboratory of Developmental Immunology, Department of Pediatrics, Massachusetts General Hospital, Harvard Medical School, Boston, Massachusetts 02114, USA. christine_kocks@hms.harvard.edu
authors.forename: Christine
authors.initials: C
authors.lastname: Kocks
authors.forename: Ju Hyun
authors.initials: JH
authors.lastname: Cho
authors.forename: Nadine
authors.initials: N
authors.lastname: Nehme
authors.forename: Johanna
authors.initials: J
authors.lastname: Ulvila
authors.forename: Alan M
authors.initials: AM
authors.lastname: Pearson
authors.forename: Marie
authors.initials: M
authors.lastname: Meister
authors.forename: Charles
authors.initials: C
authors.lastname: Strom
authors.forename: Stephanie L
authors.initials: SL
authors.lastname: Conto
authors.forename: Charles
authors.initials: C
authors.lastname: Hetru
authors.forename: Lynda M
authors.initials: LM
authors.lastname: Stuart
authors.forename: Thilo
authors.initials: T
authors.lastname: Stehle
authors.forename: Jules A
authors.initials: JA
authors.lastname: Hoffmann
authors.forename: Jean-Marc
authors.initials: JM
authors.lastname: Reichhart
authors.forename: Dominique
authors.initials: D
authors.lastname: Ferrandon
authors.forename: Mika
authors.initials: M
authors.lastname: Rämet
authors.forename: R Alan B
authors.initials: RA
authors.lastname: Ezekowitz
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D001424:Bacterial Infections / Q000517:prevention & control; D004330:Drosophila / Q000166:cytology / Q000196:embryology / Q000235:genetics / Q000382:microbiology*; D029721:Drosophila Proteins / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D004625:Embryo, Nonmammalian; D004926:Escherichia coli / Q000472:pathogenicity; D005434:Flow Cytometry; D016368:Frameshift Mutation; D017344:Genes, Insect; D006639:Histidine / Q000737:chemistry; D017403:In Situ Hybridization; D019476:Insect Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D008264:Macrophages / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D008969:Molecular Sequence Data; D016366:Open Reading Frames; D010587:Phagocytosis; D034622:RNA Interference; D012333:RNA, Messenger / Q000378:metabolism; D011956:Receptors, Cell Surface / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D017386:Sequence Homology, Amino Acid; D012706:Serratia marcescens / Q000472:pathogenicity
chemical_list: D029721:Drosophila Proteins; D019476:Insect Proteins; D008565:Membrane Proteins; D012333:RNA, Messenger; D011956:Receptors, Cell Surface; C505820:eater protein, Drosophila; D006639:Histidine