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Gene Review

BND  -  bindin

Strongylocentrotus purpuratus

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Disease relevance of BND

  • The functional domain structure of bindin, an adhesive protein component of the acrosomal granule of sea urchin sperm, has been analyzed using a series of carboxyl- and amino-terminal deletion analogs of recombinant bindin expressed in Escherichia coli [1].

High impact information on BND

  • Recombinant protein corresponding to the species-specific EBR repeat displays species-specific sperm adhesion and bindin-binding activity [2].
  • We report the isolation and sequence of bindin cDNA clones prepared from Strongylocentrotus purpuratus testis RNA [3].
  • Bindin, a major protein of the sea urchin acrosome granule, mediates the species-specific adhesion and binding of sperm to egg required to effect fertilization [3].
  • These results demonstrate that a few specific regions of the bindin molecule are involved in the sperm-egg contact and that certain of these regions mediate the species specificity of the interaction in a sequence-specific manner [4].
  • Active peptides representing certain specific subregions of the bindin sequence displayed IC50 values < 10% of the average value for control peptides, and the IC50 for the most potent of the peptides tested was only approximately 1% of the control peptide value (IC50 = 2.2 microM) [4].

Biological context of BND

  • Complementary to ongoing functional biochemical studies, I take a comparative approach to explore the molecular evolution of bindin in a group of closely related free-spawning echinoid species [5].
  • The binding of fucoidan to bindin is stable in high salt (50% at 1.2 M NaCl) whereas the binding of fucoidan to DEAE-cellulose or polylysine is inhibited by the concentrations of salt normally found in sea water (50% at 0.2 and 0.5 M NaCl, respectively) [6].
  • Thus, mode of bindin evolution is not correlated with phylogenetic affinities or molecular structure, but rather with whether the species in a genus are allopatric or sympatric [7].
  • Bindin, a sea urchin sperm protein, mediates sperm-egg attachment and membrane fusion and is thus important in species recognition and speciation [7].
  • Two new bindin cDNA sequences that contain the entire open reading frame for the binding precursor are reported: one for Strongylocentrotus franciscanus and one for Lytechinus variegatus [8].

Anatomical context of BND


Associations of BND with chemical compounds

  • Polysaccharide structural features that are critical for the binding of sulfated fucans to bindin, the adhesive protein from sea urchin sperm [6].
  • The data presented demonstrate that the sulfate esters and a molecular weight in excess of approximately 15,000 are required for high affinity binding of the fucans to bindin [6].
  • We have investigated the structural features of sulfated fucose-containing polysaccharides which are responsible for their selective binding to Strongylocentrotus purpuratus bindin [6].
  • Group-specific modification of either arginine, lysine, or histidine residues of bindin results in a substantial inactivation of fucan binding activity [12].
  • Other sulfated polysaccharides which do not interact strongly with bindin did not protect binding from phenylglyoxal-mediated inactivation when 800-3000-fold more polysaccharide than fucan was used during the preincubation before modification [12].

Analytical, diagnostic and therapeutic context of BND


  1. Structure/function analysis of the sea urchin sperm adhesive protein bindin. Lopez, A., Miraglia, S.J., Glabe, C.G. Dev. Biol. (1993) [Pubmed]
  2. The species-specific egg receptor for sea urchin sperm adhesion is EBR1,a novel ADAMTS protein. Kamei, N., Glabe, C.G. Genes Dev. (2003) [Pubmed]
  3. Sequence of mRNA coding for bindin, a species-specific sea urchin sperm protein required for fertilization. Gao, B., Klein, L.E., Britten, R.J., Davidson, E.H. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  4. Species-specific inhibition of fertilization by a peptide derived from the sperm protein bindin. Minor, J.E., Britten, R.J., Davidson, E.H. Mol. Biol. Cell (1993) [Pubmed]
  5. The molecular evolution of sperm bindin in six species of sea urchins (Echinoida: Strongylocentrotidae). Biermann, C.H. Mol. Biol. Evol. (1998) [Pubmed]
  6. Polysaccharide structural features that are critical for the binding of sulfated fucans to bindin, the adhesive protein from sea urchin sperm. DeAngelis, P.L., Glabe, C.G. J. Biol. Chem. (1987) [Pubmed]
  7. Evolution of bindin in the pantropical sea urchin Tripneustes: comparisons to bindin of other genera. Zigler, K.S., Lessios, H.A. Mol. Biol. Evol. (2003) [Pubmed]
  8. Comparison of the bindin proteins of Strongylocentrotus franciscanus, S. purpuratus, and Lytechinus variegatus: sequences involved in the species specificity of fertilization. Minor, J.E., Fromson, D.R., Britten, R.J., Davidson, E.H. Mol. Biol. Evol. (1991) [Pubmed]
  9. Locale and level of bindin mRNA in maturing testis of the sea urchin, Strongylocentrotus purpuratus. Cameron, R.A., Minor, J.E., Nishioka, D., Britten, R.J., Davidson, E.H. Dev. Biol. (1990) [Pubmed]
  10. Evaluation of sequence variation and selection in the bindin locus of the red sea urchin, Strongylocentrotus franciscanus. Debenham, P., Brzezinski, M.A., Foltz, K.R. J. Mol. Evol. (2000) [Pubmed]
  11. Purification of sea urchin sperm bindin by DEAE-cellulose chromatography. Vacquier, V.D. Anal. Biochem. (1983) [Pubmed]
  12. Role of basic amino acids in the interaction of bindin with sulfated fucans. DeAngelis, P.L., Glabe, C.G. Biochemistry (1988) [Pubmed]
  13. Localization of bindin expression during sea urchin spermatogenesis. Nishioka, D., Ward, R.D., Poccia, D., Kostacos, C., Minor, J.E. Mol. Reprod. Dev. (1990) [Pubmed]
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