Mouse sperm exhibit chemotaxis to allurin, a truncated member of the cysteine-rich secretory protein family

Lindsey A. Burnett, Douglas M. Anderson, Alan Rawls, Allan L. Bieber, Douglas E. Chandler

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


Allurin, a 21. kDa protein isolated from egg jelly of the frog Xenopus laevis, has previously been demonstrated to attract frog sperm in two-chamber and microscopic assays. cDNA cloning and sequencing has shown that allurin is a truncated member of the Cysteine-Rich Secretory Protein (CRISP) family, whose members include mammalian sperm-binding proteins that have been postulated to play roles in spermatogenesis, sperm capacitation and sperm-egg binding in mammals. Here, we show that allurin is a chemoattractant for mouse sperm, as determined by a 2.5-fold stimulation of sperm passage across a porous membrane and by analysis of sperm trajectories within an allurin gradient as observed by time-lapse microscopy. Chemotaxis was accompanied by an overall change in trajectory from circular to linear thereby increasing sperm movement along the gradient axis. Allurin did not increase sperm velocity although it did produce a modest increase in flagellar beat frequency. Oregon Green 488-conjugated allurin was observed to bind to the sub-equatorial region of the mouse sperm head and to the midpiece of the flagellum. These findings demonstrate that sperm have retained the ability to bind and respond to truncated Crisp proteins over 300. million years of vertebrate evolution.

Original languageEnglish (US)
Pages (from-to)318-328
Number of pages11
JournalDevelopmental Biology
Issue number2
StatePublished - Dec 15 2011


  • Crisp proteins
  • Fertilization
  • Frog egg jelly
  • Reproductive protein evolution
  • Sperm chemotaxis
  • Sperm motility

ASJC Scopus subject areas

  • Molecular Biology
  • Developmental Biology
  • Cell Biology


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