ArticleThe Journal of cell biology1997
Gamete interactions in Xenopus laevis: identification of sperm binding glycoproteins in the egg vitelline envelope.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
17 citing papers in PubMed, 98 citations in OpenAlex.
- TheBiomolecules · 2025Review
- Article
- Effects of short-term exposure of paracetamol in the gonads of blue mussels Mytilus edulis.Environmental science and pollution research international · 2020Article
- Glycan-Independent Gamete Recognition Triggers Egg Zinc Sparks and ZP2 Cleavage to Prevent Polyspermy.Developmental cell · 2018Article
- Egg Coat Proteins Across Metazoan Evolution.Current topics in developmental biology · 2018Review
- Phospholipase C and D regulation of Src, calcium release and membrane fusion during Xenopus laevis development.Developmental biology · 2015Review
- Transmembrane signal transduction in oocyte maturation and fertilization: focusing on Xenopus laevis as a model animal.International journal of molecular sciences · 2014Review
- 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
- Marine glycobiology: current status and future perspectives.Marine biotechnology (New York, N.Y.) · 2010Review
- Dicalcin inhibits fertilization through its binding to a glycoprotein in the egg envelope in Xenopus laevis.The Journal of biological chemistry · 2010Article
- The envelopes of amphibian oocytes: physiological modifications in Bufo arenarum.Reproductive biology and endocrinology : RB&E · 2003Article
- Allurin, a 21-kDa sperm chemoattractant from Xenopus egg jelly, is related to mammalian sperm-binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- O-glycan variability of egg-jelly mucins from Xenopus laevis: characterization of four phenotypes that differ by the terminal glycosylation of their mucins.The Biochemical journal · 2000Article
- Xenopus laevis sperm receptor gp69/64 glycoprotein is a homolog of the mammalian sperm receptor ZP2.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
- Xenopus Cdc6 confers sperm binding competence to oocytes without inducing their maturation.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- The abalone egg vitelline envelope receptor for sperm lysin is a giant multivalent molecule.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
A quantitative assay was developed to study the interaction of Xenopus laevis sperm and eggs. Using this assay it was found that sperm bound in approximately equal numbers to the surface of both hemispheres of the unfertilized egg, but not to the surface of the fertilized egg. To understand the molecular basis of sperm binding to the egg vitelline envelope (VE), a competition assay was used and it was found that solubilized total VE proteins inhibited sperm-egg binding in a concentration-dependent manner. Individual VE proteins were then isolated and tested for their ability to inhibit sperm binding. Of the seven proteins in the VE, two related glycoproteins, gp69 and gp64, inhibited sperm-egg binding. Polyclonal antibody was prepared that specifically recognized gp69 and gp64. This gp69/64 specific antibody bound to the VE surface and blocked sperm binding, as well as fertilization. Moreover, agarose beads coated with gp69/64 showed high sperm binding activity, while beads coated with other VE proteins bound few sperm. Treatment of unfertilized eggs with crude collagenase resulted in proteolytic modification of only the gp69/64 components of the VE, and this modification abolished sperm-egg binding. Small glycopeptides generated by Pronase digestion of gp69/64 also inhibited sperm-egg binding and this inhibition was abolished by treatment of the glycopeptides with periodate. Based on these observations, we conclude that the gp69/64 glycoproteins in the egg vitelline envelope mediate sperm-egg binding, an initial step in Xenopus fertilization, and that the oligosaccharide chains of these glycoproteins may play a critical role in this process.
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Registered trials
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