title: Identification of protein components of egg masses indicates parental investment in immunoprotection of offspring by Biomphalaria glabrata (gastropoda, mollusca).
abstract: The macromolecules contributed by the freshwater gastropod Biomphalaria glabrata, intermediate host of Schistosoma mansoni, to developing offspring inside egg masses are poorly known. SDS-PAGE fractionated egg mass fluids (EMF) of M line and BB02 B. glabrata were analyzed by MALDI-TOF (MS and tandem MS). A MASCOT database was assembled with EST data from B. glabrata and other molluscs to aid in sequence characterization. Of approximately 20 major EMF polypeptides, 16 were identified as defense-related, including protease inhibitors, a hemocyanin-like factor and tyrosinase (each with possible phenoloxidase activity), extracellular Cu-Zn SOD, two categories of C-type lectins, Gram-negative bacteria-binding protein (GNBP), aplysianin/achacin-like protein, as well as versions of lipopolysaccharide binding protein/bacterial permeability-increasing proteins (LBP/BPI) that differed from those previously described from hemocytes. Along with two sequences that were encoded by "unknown" ESTs, EMF also yielded a compound containing a vWF domain that is likely involved in defense and a polypeptide with homology to the Aplysia pheromone temptin. Further study of B. glabrata pheromones is warranted as these could be useful in efforts to control these schistosome-transmitting snails. Several of the EMF polypeptides were contained in the albumen gland, the organ that produces most EMF. Thus, parental investment of B. glabrata in immunoprotection of its offspring is indicated to be considerable.
authors.affiliation: Center for Evolutionary and Theoretical Immunology, Department of Biology, University of New Mexico, MSC03 2020, Albuquerque, NM 87131, USA.
authors.forename: Jennifer J M
authors.initials: JJ
authors.lastname: Hathaway
authors.forename: Coen M
authors.initials: CM
authors.lastname: Adema
authors.forename: Barbara A
authors.initials: BA
authors.lastname: Stout
authors.forename: Charlotte D
authors.initials: CD
authors.lastname: Mobarak
authors.forename: Eric S
authors.initials: ES
authors.lastname: Loker
mesh_terms: D000209:Acute-Phase Proteins / Q000276:immunology; D000595:Amino Acid Sequence; D000818:Animals; D001048:Aplysia / Q000502:physiology; D001700:Biomphalaria / Q000469:parasitology / Q000502:physiology*; D002352:Carrier Proteins / Q000276:immunology; D004527:Egg Proteins / Q000276:immunology / Q000378:metabolism*; D007113:Immunity, Innate; D008562:Membrane Glycoproteins / Q000276:immunology; D008969:Molecular Sequence Data; D014442:Monophenol Monooxygenase / Q000276:immunology; D010675:Pheromones / Q000276:immunology; D040901:Proteomics; D012098:Reproduction; D012550:Schistosoma mansoni / Q000276:immunology; D012555:Schistosomiasis mansoni / Q000276:immunology*; D017386:Sequence Homology, Amino Acid; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013482:Superoxide Dismutase / Q000276:immunology; D000099231:Lipopolysaccharide-Binding Protein
chemical_list: D000209:Acute-Phase Proteins; D002352:Carrier Proteins; D004527:Egg Proteins; D008562:Membrane Glycoproteins; D014442:Monophenol Monooxygenase; D010675:Pheromones; D013482:Superoxide Dismutase; D000099231:Lipopolysaccharide-Binding Protein