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Updated: Nov 25, 2025

Mechanical Separation and Protein Solubilization of the Outer and Inner Perivitelline Sublayers from Hen's Eggs
Published on: January 27, 2021
Cellular and molecular modification of egg envelope hardening in fertilization
Yeke Wang1, Feng Chen1, Jun He2
1Donghu Experimental Station of Lake Ecosystems, State Key Laboratory of Freshwater Ecology and Biotechnology, Institute of Hydrobiology, Chinese Academy of Sciences, Wuhan, 430072, China; University of Chinese Academy of Sciences, Beijing, 100049, China.
Abstract:
Fertilization is an essential process that fundamentally impacts fitness. An egg changes dramatically after fertilization mediating the beginning of life, which mainly includes the transformation of the egg envelope via hardening, which is thought to be due to complex reactions involved in the conversion of cellular and molecular. This review highlights the mechanisms of egg envelope hardening in teleost fish. We conclude that the egg envelope hardening might be carried out in two steps. (a) A metalloprotease (alveolin) hydrolyzes the N-terminal proline-glutamine (Pro-Gln) region of zona pellucida (ZP) 1 and (b) triggers intermolecular cross-linking to ZP3 catalyzed by transglutaminase (TGase). The post-fertilization hardening of the egg envelope is an evolutionarily conserved phenomenon across species. We discuss the biochemical function and interaction of some factors reported to be essential to egg envelope hardening in mammalian and nonmammalian species, including metalloprotease, TGase, peroxidase/ovoperoxidase, and other factors (carbohydrate moieties, zinc and Larp6 proteins), and the relevant data suggest that egg envelope hardening is crucial to block polyspermy in internal fertilization, in addition to protecting the developing embryo from mechanical shock and preventing bacterial infection in external fertilization. Increased knowledge of the processes of egg envelope hardening and fertilization is likely to make a remarkable contribution to reproduction and aquaculture.
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