Biochim Biophys Acta 1990 Jan 19;10371:100-5. doi: 10.1016/0167-4838(90)90107-q.

Specific recognition of sulfate esters by bindin, a sperm adhesion protein from sea urchins.

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Bindin specifically binds to egg surface sulfated fucan polysaccharides and mediates the attachment of sperm to the egg during fertilization. Sulfate esters are critical for this interaction. We have examined the effect of different anionic groups on the relative binding affinities of a series of homologous anionic polymers for bindin to determine the extent to which other charged moieties can substitute for sulfate. We found that bindin displays a remarkable specificity for sulfate- or sulfonic acid-containing polymers. The relative affinities of poly(vinyl sulfate) and poly(styrenesulfonic acid) are four orders of magnitude higher than polymers containing phosphate esters or carboxyl groups. The bindin-mediated aggregation of sea urchin eggs was inhibited by the sulfated polymers but not the other anionic polymers. This high degree of selectivity for sulfated polymers is not observed for the binding of the polyanions to most other proteins and basic polypeptides. These results suggest that the binding is not due to the formation of simple salt bridges, and that all three non-ester oxygen atoms of the sulfate groups are involved in multiple bonding interactions with a complementary ''docking site'' on the bindin polypeptide. The orientation of the polysaccharide sulfate oxygen atoms relative to the protein binding site may be an important determinant of the specificity of polysaccharide binding.

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Genes referenced: bindin LOC100887844