Allurin, an Amphibian Sperm Chemoattractant Having Implications for Mammalian Sperm Physiology

Lindsey A. Burnett, Catherine A. Washburn, Hitoshi Sugiyama, Xueyu Xiang, John H. Olson, Bader Al-Anzi, Allan L. Bieber, Douglas E. Chandler

Research output: Contribution to journalArticlepeer-review

6 Scopus citations


Eggs of many species are surrounded by extracellular coats that emit ligands to which conspecific sperm respond by undergoing chemotaxis and changes in metabolism, motility, and acrosomal status in preparation for fertilization. Here we review methods used to measure sperm chemotaxis and focus on recent studies of allurin, a 21-kDa protein belonging to the Cysteine-RIch Secretory Protein (CRISP) family that has chemoattraction activity for both amphibian and mammalian sperm. Allurin is unique in being the first extensively characterized Crisp protein found in the female reproductive tract and is the product of a newly discovered amphibian gene within a gene cluster that has been largely conserved in mammals. Study of its expression, function, and tertiary structure could lead to new insights in the role of Crisp proteins in sperm physiology.

Original languageEnglish (US)
Pages (from-to)1-61
Number of pages61
JournalInternational Review of Cell and Molecular Biology
StatePublished - 2012


  • Crisp proteins
  • Egg jelly
  • Fertilization
  • Sperm chemoattraction
  • Xenopus laevis

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology
  • Biochemistry


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