ArticleProceedings of the National Academy of Sciences of the United States of America1998
Inactivation of the mouse sperm receptor, mZP3, by site-directed mutagenesis of individual serine residues located at the combining site for sperm.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Molecular interplay between sperm and oocyte: a narrative review.Human reproduction update · 2026Review
- Mutational disruption of transcription factors binding and regulatory networks in a case of unexplained total fertilization failure.Journal of translational medicine · 2025Article
- Improving sperm selection strategies for assisted reproduction through closing the knowledge gap in sperm maturation mechanics.Human reproduction open · 2025Review
- Article
- The Novel Role ofInternational journal of molecular sciences · 2023Article
- Plant-Produced Mouse-Specific Zona Pellucida 3 Peptide Induces Immune Responses in Mice.Vaccines · 2023Article
- Article
- Human Zona Pellucida Glycoproteins: Binding Characteristics With Human Spermatozoa and Induction of Acrosome Reaction.Frontiers in cell and developmental biology · 2021Review
- Mammalian egg coat modifications and the block to polyspermy.Molecular reproduction and development · 2020Review
- Article
- Egg Coat Proteins Across Metazoan Evolution.Current topics in developmental biology · 2018Review
- Gamete compatibility genes in mammals: candidates, applications and a potential path forward.Royal Society open science · 2017Review
- ZP3 is Required for Germinal Vesicle Breakdown in Mouse Oocyte Meiosis.Scientific reports · 2017Article
- A single domain of the ZP2 zona pellucida protein mediates gamete recognition in mice and humans.The Journal of cell biology · 2014Article
- The maternal to zygotic transition in mammals.Molecular aspects of medicine · 2013Review
- The molecular basis of gamete recognition in mice and humans.Molecular human reproduction · 2013Review
- Human sperm bind to the N-terminal domain of ZP2 in humanized zonae pellucidae in transgenic mice.The Journal of cell biology · 2012Article
- Structure of betaglycan zona pellucida (ZP)-C domain provides insights into ZP-mediated protein polymerization and TGF-beta binding.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- The Tn antigen-structural simplicity and biological complexity.Angewandte Chemie (International ed. in English) · 2011Review
- Acrosome reaction: relevance of zona pellucida glycoproteins.Asian journal of andrology · 2011Review
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To initiate fertilization, mouse sperm bind to Ser- (O-) linked oligosaccharides located at the sperm combining site of zona pellucida glycoprotein mZP3. Apparently, the oligosaccharides are present on one or more of five Ser residues clustered in the carboxyl-terminal region of the mZP3 polypeptide. Here, each of the Ser residues, as well as an intervening Asn residue, was converted to a small, nonhydroxy amino acid by site-directed mutagenesis. Mouse embryonal carcinoma (EC) cells were then stably transfected with the wild-type and mutated mZP3 genes. In each case, transfected cells synthesized and secreted recombinant EC-mZP3 into the culture medium. The glycoproteins were partially purified and assayed for their ability to inhibit binding of sperm to ovulated eggs in vitro. As compared with wild-type EC-mZP3, mutations of Ser-329, Ser-331, or Ser-333 had no effect on sperm receptor activity. Mutation of Asn-330, a potential N-linked glycosylation site, also had no effect on sperm receptor activity. On the other hand, mutation of either Ser-332 or Ser-334, or mutation of Ser-332, Ser-333, and Ser-334, resulted in complete inactivation of EC-mZP3 as a sperm receptor. These results suggest that Ser-332 and Ser-334, residues conserved in mouse, hamster, and human ZP3, are essential for sperm receptor activity.
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