Structure and function of the proteins of the mammalian zona pellucida

The zona pellucida (ZP) is the extracellular matrix that plays important ro les in sperm-egg interaction. The ZP is composed of three major glycoprotei ns that exhibit heterogeneity due to extensive post-translational modificat ions including glycosylation and sulfation. Because of these modifications the nomenclature of ZP proteins from different species based on electrophor etic mobilities has been confusing. As the cDNAs and genes encoding the dif ferent ZP proteins have been isolated and sequenced, it is now possible to relate these ZP proteins according to gene families. Using the mouse ZP nom enclature, the ZP proteins from different mammalian species can be classifi ed into three protein families: ZP1, ZP2, and ZP3. Although some of the str uctural domains of the ZP proteins of different species are conserved withi n each family, they exhibit distinct biological properties. In the mouse it has been established that ZP3 is the primary sperm receptor while ZP2 has secondary sperm receptor properties. In the pig, however, ZP1 has been show n to have sperm receptor activity similar to that observed in the rabbit an d nonhuman primates. It is of interest that the human ZP2 and ZP3 gene fami lies are 60-70% conserved with respect to the mouse ZP amino acid sequence, while the mouse ZP1 is only 39% conserved with respect to human ZP1. Such differences in protein structure and glysosylation may explain the marked s pecies differences in the biochemical, physicochemical and immunochemical p roperties of the ZP. Studies have now shown that the proteins of the ZP are expressed in a stage specific manner and that there is increasing evidence that ZP proteins are expressed by both granulosa cells and the oocyte and may play a role in granulosa cell differentiation. Copyright (C) 2000 S. Karger AG. Basel.