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

作者：Burnett Lindsey A; Anderson Douglas M; Rawls Alan; Bieber Allan L; Chandler Douglas E^*

来源：Developmental Biology, 2011, 360(2): 318-328.

DOI：10.1016/j.ydbio.2011.09.028

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

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 subequatorial 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.

• 出版日期2011-12-15