6533b85afe1ef96bd12b8cb6
RESEARCH PRODUCT
Bio-sintering processes in hexactinellid sponges: Fusion of bio-silica in giant basal spicules from Monorhaphis chuni☆
Werner E. G. M�llerMatthias WiensAlexandra BoreikoJoachim BillXiaohong WangAnatoli KraskoUte SchlossmacherZaklina BurghardHeinz C. Schrödersubject
FusionSpiculebiologyHexactinellidMolecular Sequence DataAnimal StructuresAnatomyBlotting NorthernSilicon Dioxidebiology.organism_classificationPoriferaSpongeLamella (surface anatomy)Sponge spiculeStructural BiologySpectrometry Mass Matrix-Assisted Laser Desorption-IonizationComplementary DNAMicroscopy Electron ScanningBiophysicsAnimalsLamellar structuredescription
The two sponge classes, Hexactinellida and Demospongiae, comprise a skeleton that is composed of siliceous skeletal elements (spicules). Spicule growth proceeds by appositional layering of lamellae that consist of silica nanoparticles, which are synthesized via the sponge-specific enzyme silicatein. While in demosponges during maturation the lamellae consolidate to a solid rod, the lamellar organization of hexactinellid spicules largely persists. However, the innermost lamellae, near the spicule core, can also fuse to a solid axial cylinder. Similar to the fusion of siliceous nanoparticles and lamella, in several hexactinellid species individual spicules unify during sintering-like processes. Here, we study the different stages of a process that we termed bio-sintering, within the giant basal spicule (GBS) of Monorhaphis chuni. During this study, a major GBS protein component (27 kDa) was isolated and analyzed by MALDI-TOF-MS. The sequences were used to isolate and clone the encoding cDNA via degenerate primer PCR. Bioinformatic analyses revealed a significant sequence homology to silicatein. In addition, the native GBS protein was able to mediate bio-silica synthesis in vitro. We conclude that the syntheses of bio-silica in M. chuni, and the subsequent fusion of nanoparticles to lamellae, and finally to spicules, are enzymatically-driven by a silicatein-like protein. In addition, evidence is now presented that in hexactinellids those fusions involve sintering-like processes.
year | journal | country | edition | language |
---|---|---|---|---|
2009-05-16 | Journal of Structural Biology |