Publications: Peer-reviewed journal articles (by staff)

Extraordinary intraspecific diversity in oyster sperm bindin

  • Moy GW,
  • Springer SA,
  • Adams SL,
  • Swanson WJ,
  • and Vacquier VD
1 January, 2008

Moy GW, Springer SA, Adams SL, Swanson WJ, Vacquier VD 2008. Extraordinary intraspecific diversity in oyster sperm bindin. PNAS 105(6): 1993-1998.


In free-spawning invertebrates sperm-egg incompatibility is a barrier to mating between species, and divergence of gamete recognition proteins (GRPs) can result in reproductive isolation. Of interest are processes that create reproductive protein diversity within species, because intraspecific variants are potentially involved in mate choice and early speciation. Sperm acrosomes of the Pacific oyster Crassostrea gigas contain the protein bindin that bonds sperm to egg during fertilization. Oyster bindin is a single-copy gene encoding a diversity of protein variants. Oyster bindins have a conserved N-terminal region followed by one to five tandem fucose-binding lectin (F-lectin) domains. These repeats have diversified by positive selection at eight sites clustered on the F-lectin's fucose binding face. Additional bindin variants result from recombination in an intron in each F-lectin repeat. Males also express alternatively spliced bind in cDNAs with one to five repeats, but typically translate only one or two isoforms into protein. Thus, positive selection, alternative splicing, and recombination can create thousands of bindin variants within C gigas. Models of sexual conflict predict high male diversity when females are diverse and sexual conflict is strong. The amount of intraspecific polymorphism in male GRPs may be a consequence of the relative efficiency of local (molecular recognition) and global (electrical, cortical, and physical) polyspermy blocks that operate during fertilization.