Females of the sea urchin Strongylocentrotus purpuratus differ in the structures of their egg jelly sulfated fucans

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Abstract
The egg jelly coats of sea urchins contain sulfated fucans which bind to a sperm surface receptor glycoprotein to initiate the signal transduction events resulting in the sperm acrosome reaction. The acrosome reaction is an ion channel regulated exocytosis which is an obligatory event for sperm binding to, and fusion with, the egg. Approximately 90% of individual females of the sea urchin Strongylocentrotus purpuratus spawned eggs having only one of two possible sulfated fucan electrophoretic isotypes, a slow migrating (sulfated fucan I), or a fast migrating (sulfated fucan II) isotype. The remaining 10% of females spawned eggs having both sulfated fucan isotypes. The two sulfated fucan isotypes were purified from egg jelly coats and their structures determined by NMR spectroscopy and methylation analysis. Both sulfated fucans are linear polysaccharides composed of 1→3-linked α-l-fucopyranosyl units. Sulfated fucan I is entirely sulfated at the O-2 position but with a heterogeneous sulfation pattern at O-4 position. Sulfated fucan II is composed of a regular repeating sequence of 3 residues, as follows: [3-α-l-Fucp-2,4(OSO3)-1→3-α-l-Fucp-4(OSO3)-1→3-α-l-Fucp-4(OSO3)-1]n. Both purified sulfated fucans have approximately equal potency in inducing the sperm acrosome reaction. The significance of two structurally different sulfated fucans in the egg jelly coat of this species could relate to the finding that the sperm receptor protein which binds sulfated fucan contains two carbohydrate recognition modules of the C-type lectin variety which differ by 50% in their primary structure.