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Sperm lacking Bindin are infertile but are otherwise indistinguishable from wildtype sperm
Gary M Wessel1, Yuuko Wada2, Mamiko Yajima3
1Division of BioMed, Department of Molecular and Cellular Biology and Biochemistry, Brown University, 185 Meeting Street, Providence, RI, 02912, USA. rhet@brown.edu.
Scientific Reports
|November 4, 2021
Summary
Sea urchin sperm protein Bindin is crucial for fertilization, enabling species-specific sperm-egg interactions. Sperm lacking Bindin cannot fertilize eggs but otherwise function normally, indicating Bindin
Area of Science:
- Reproductive Biology
- Developmental Biology
- Molecular Genetics
Background:
- Cell-cell fusion is a specialized process, with sperm-egg fusion during fertilization being a key example.
- Gamete-specific proteins on sperm surfaces mediate species-specific interactions with eggs.
- Bindin is a sea urchin sperm protein essential for binding to homologous eggs.
Purpose of the Study:
- To investigate the phenotypic consequences of Bindin absence in sea urchin sperm.
- To confirm the role of Bindin exclusively in species-specific sperm-egg interactions.
Main Methods:
- Utilized Cas9 targeted gene inactivation in the sea urchin Hemicentrotus pulcherrimus to create Bindin-minus sperm.
- Analyzed sperm morphology, function (including acrosomal reaction), and binding/fertilization capacity.
- Observed the development and metamorphosis of embryos produced by Bindin-minus sperm.
Main Results:
- Bindin-minus sperm exhibited normal morphology and function, including head shape, tail motility, and acrosomal reaction.
- Sperm lacking Bindin failed to bind to or fertilize eggs, even at high concentrations.
- Bindin-minus embryos developed into normal, fertile adults, indicating no other biological roles for Bindin.
Conclusions:
- Bindin is essential and sufficient for species-specific sperm-egg recognition and fusion in sea urchins.
- The function of Bindin is strictly limited to gamete interaction, not affecting sperm viability or other developmental processes.
- Evolutionary changes in Bindin are not constrained by other cellular functions, allowing for rapid divergence.
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