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A Protocol for Bioinspired Design: A Ground Sampler Based on Sea Urchin Jaws
Published on: April 24, 2016
Glycosylation Fosters Interactions between Model Sea Urchin Spicule Matrix Proteins. Implications for Embryonic
Gaurav Jain1, Martin Pendola1, Eleni Koutsoumpeli2
1Laboratory for Chemical Physics, Center for Skeletal and Craniofacial Biology , New York University , 345 East 24th Street , New York , New York 10010 , United States.
Abstract:
The formation of embryonic mineralized skeletal elements (spicules) in the sea urchin requires the participation of proteins, many of which may interact with one another and assist in the creation of an extracellular matrix wherein mineral formation takes place. To probe this, we created a sea urchin spicule recombinant model protein pair system wherein we tested the interactions between two major spicule proteins, SpSM50 and the glycoprotein, SpSM30B/C. Both proteins are strong hydrogelators that manipulate early and later events in mineral formation. We discovered that the anionic glycan moieties of SpSM30B/C are required for interaction with the SpSM50 protein and that these interactions are Ca(II)-independent. In addition, when these proteins form a complex, they create hybrid hydrogel particles that are physically distinct from their individual counterparts. Thus, glycan-mediated interactions play an important role in in vitro spicule protein assembly and most likely within the spicule itself.
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