Fusion between gametes is a key event in the fertilization process involving the interaction of specific domains of the sperm and egg plasma membranes. During recent years, efforts have been made toward the identification of the specific molecular components involved in this event. The present work will focus on the best characterized candidates for mediating gamete membrane fusion in mammals. These molecules include members of the ADAM (a disintegrin and a metalloprotease domain) family, i.e., testicular proteins fertilin α, fertilin β, and cyritestin, which are thought to interact with integrins in the egg plasma membrane through their disintegrin domains, and a member of the cysteine-rich secretory proteins (CRISP) family, i.e., epididymal protein DE, which participates in an event subsequent to sperm-egg binding and leading to fusion through specific complementary sites localized on the fusogenic area of the egg surface. The identification and characterization of these molecules will contribute not only to a better understanding of the molecular mechanisms underlying mammalian sperm-egg fusion but also to the development of new methods for both fertility regulation and diagnosis and treatment of human infertility.
Bibliographical noteFunding Information:
DAE and DB are Research Fellowship recipients from the National Research Council of Argentina (CONICET), MM and VR are Fellowship recipients from PLACIRH, and PSC is a Research Career Award recipient from CONICET. This work was supported by WHO grant H9/181/R429, CONRAD grant MFG- 97-29, and the National Ministry of Health grants to PSC and PLACIRH Re-Entry Grant PRE-014/97 and PRE-028/99 to DAE and DJC, respectively.
- Sperm-egg binding