title: Parental transfer of the antimicrobial protein LBP/BPI protects Biomphalaria glabrata eggs against oomycete infections.
abstract: Vertebrate females transfer antibodies via the placenta, colostrum and milk or via the egg yolk to protect their immunologically immature offspring against pathogens. This evolutionarily important transfer of immunity is poorly documented in invertebrates and basic questions remain regarding the nature and extent of parental protection of offspring. In this study, we show that a lipopolysaccharide binding protein/bactericidal permeability increasing protein family member from the invertebrate Biomphalaria glabrata (BgLBP/BPI1) is massively loaded into the eggs of this freshwater snail. Native and recombinant proteins displayed conserved LPS-binding, antibacterial and membrane permeabilizing activities. A broad screening of various pathogens revealed a previously unknown biocidal activity of the protein against pathogenic water molds (oomycetes), which is conserved in human BPI. RNAi-dependent silencing of LBP/BPI in the parent snails resulted in a significant reduction of reproductive success and extensive death of eggs through oomycete infections. This work provides the first functional evidence that a LBP/BPI is involved in the parental immune protection of invertebrate offspring and reveals a novel and conserved biocidal activity for LBP/BPI family members.
authors.affiliation: Sophia Agrobiotech Institute, INRA-CNRS-UNS, Sophia Antipolis, France ; Institut de Biologie Moléculaire et Cellulaire, UPR9022 CNRS, Strasbourg, France.
authors.forename: Olga Lucia
authors.initials: OL
authors.lastname: Baron
authors.affiliation: Aberdeen Oomycete Laboratory, University of Aberdeen, Institute of Medical Sciences, Foresterhill, Aberdeen, United Kingdom.
authors.forename: Pieter
authors.initials: P
authors.lastname: van West
authors.affiliation: Sophia Agrobiotech Institute, INRA-CNRS-UNS, Sophia Antipolis, France.
authors.forename: Benoit
authors.initials: B
authors.lastname: Industri
authors.affiliation: Sophia Agrobiotech Institute, INRA-CNRS-UNS, Sophia Antipolis, France.
authors.forename: Michel
authors.initials: M
authors.lastname: Ponchet
authors.affiliation: Sophia Agrobiotech Institute, INRA-CNRS-UNS, Sophia Antipolis, France.
authors.forename: Géraldine
authors.initials: G
authors.lastname: Dubreuil
authors.affiliation: Ecologie et Evolution des Interactions, UMR 5244 CNRS, Université de Perpignan Via Domitia, Perpignan, France.
authors.forename: Benjamin
authors.initials: B
authors.lastname: Gourbal
authors.affiliation: Institut de Biologie Moléculaire et Cellulaire, UPR9022 CNRS, Strasbourg, France.
authors.forename: Jean-Marc
authors.initials: JM
authors.lastname: Reichhart
authors.affiliation: Sophia Agrobiotech Institute, INRA-CNRS-UNS, Sophia Antipolis, France.
authors.forename: Christine
authors.initials: C
authors.lastname: Coustau
mesh_terms: D000209:Acute-Phase Proteins / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology; D001700:Biomphalaria / Q000235:genetics / Q000276:immunology / Q000378:metabolism / Q000469:parasitology; D001798:Blood Proteins / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology; D002352:Carrier Proteins / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism; D002463:Cell Membrane Permeability / Q000187:drug effects; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000187:drug effects / Q000254:growth & development / Q000378:metabolism / Q000648:ultrastructure; D005260:Female; D007112:Immunity, Maternally-Acquired / Q000235:genetics; D007239:Infections / Q000235:genetics / Q000276:immunology* / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism* / Q000494:pharmacology; D008826:Microbial Sensitivity Tests; D009868:Oomycetes / Q000187:drug effects / Q000276:immunology / Q000472:pathogenicity; D011994:Recombinant Proteins / Q000494:pharmacology; D015053:Zygote / Q000276:immunology / Q000378:metabolism / Q000469:parasitology; D000099231:Lipopolysaccharide-Binding Protein
chemical_list: D000209:Acute-Phase Proteins; D023181:Antimicrobial Cationic Peptides; D001798:Blood Proteins; D002352:Carrier Proteins; D008562:Membrane Glycoproteins; D011994:Recombinant Proteins; D000099231:Lipopolysaccharide-Binding Protein; C021623:bactericidal permeability increasing protein