title: The shell matrix of the pulmonate land snail Helix aspersa maxima.
abstract: In mollusks, the shell mineralization process is controlled by an array of proteins, glycoproteins and polysaccharides that collectively constitute the shell matrix. In spite of numerous researches, the shell protein content of a limited number of model species has been investigated. This paper presents biochemical data on the common edible land snail Helix aspersa maxima, a model organism for ecotoxicological purposes, which has however been poorly investigated from a biomineralization viewpoint. The shell matrix of this species was extracted and analyzed biochemically for functional in vitro inhibition assay, for amino acid and monosaccharides compositions. The matrix was further analyzed on 1 and 2D gels and short partial protein sequences were obtained from 2D gel spots. Serological comparisons were established with a set of heterologous antibodies, two of which were subsequently used for subsequent immunogold localization of matrix components. Our data suggest that the shell matrix of Helix aspersa maxima may differ widely from the shell secretory repertoire of the marine mollusks studied so far, such as the gastropod Haliotis or the pearl oyster Pinctada. In particular, most of the biochemical properties generally attributed to soluble shell matrices, such as calcium-binding capability, or the capacity to interfere in vitro with the precipitation of calcium carbonate or to inhibit the precipitation of calcium carbonate, were not recorded with this matrix. This drastic change in the biochemical properties of the landsnail shell matrix puts into question the existence of a unique molecular model for molluscan shell formation, and may be related to terrestrialisation.
authors.affiliation: UMR 5561 CNRS Biogéosciences, Université de Bourgogne, 6 Bd. Gabriel, F-21000 Dijon, France.
authors.forename: Céline
authors.initials: C
authors.lastname: Pavat
authors.forename: Isabelle
authors.initials: I
authors.lastname: Zanella-Cléon
authors.forename: Michel
authors.initials: M
authors.lastname: Becchi
authors.forename: Davorin
authors.initials: D
authors.lastname: Medakovic
authors.forename: Gilles
authors.initials: G
authors.lastname: Luquet
authors.forename: Nathalie
authors.initials: N
authors.lastname: Guichard
authors.forename: Gérard
authors.initials: G
authors.lastname: Alcaraz
authors.forename: Jean-Louis
authors.initials: JL
authors.lastname: Dommergues
authors.forename: Antoine
authors.initials: A
authors.lastname: Serpentini
authors.forename: Jean-Marc
authors.initials: JM
authors.lastname: Lebel
authors.forename: Frédéric
authors.initials: F
authors.lastname: Marin
mesh_terms: D000596:Amino Acids / Q000032:analysis; D060105:Animal Shells / Q000737:chemistry* / Q000648:ultrastructure; D000818:Animals; D002119:Calcium Carbonate / Q000737:chemistry; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D005602:France; D006372:Helix, Snails / Q000737:chemistry*; D007150:Immunohistochemistry; D008855:Microscopy, Electron, Scanning; D009005:Monosaccharides / Q000032:analysis; D011506:Proteins / Q000032:analysis*; D013045:Species Specificity; D053719:Tandem Mass Spectrometry; D014961:X-Ray Diffraction
chemical_list: D000596:Amino Acids; D009005:Monosaccharides; D011506:Proteins; D002119:Calcium Carbonate