Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 399, Issue 3, Pages 406-411Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2010.07.088
Keywords
Binder-of-sperm (BSP) proteins; Sperm; Membranes; Protrusions; Nanotubes; Fluorescence microscopy; Cryo-electron microscopy; Lipids; Lipid curvature; Lipid morphology
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Funding
- Natural Sciences and Engineering Council of Canada
- Fonds Quebecois de la Recherche sur la Nature et les Technologies of Quebec
- Swedish Research Council
- Royal Academy of Arts and Sciences of Uppsala
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Binder-of-sperm (BSP) proteins interact with sperm membranes and are proposed to extract selectively phosphatidylcholine and cholesterol from these. This change in lipid composition is a key step in sperm capacitation. The present work demonstrates that the interactions between the protein BSP1 and model membranes composed with phosphatidylcholine lead to drastic changes in the morphology of the lipidic self-assemblies. Using cryo-electron microscopy and fluorescence microscopy, we show that, in the presence of the protein, the lipid vesicles elongate, and form bead necklace-like structures that evolve toward small vesicles or thread-like structures. In the presence of multilamellar vesicles, where a large reservoir of lipid is available, the presence of BSP proteins lead to the formation of long nanotubes. Long spiral-like threads, associated with lipid/protein complexes, are also observed. The local curvature of lipid membranes induced by the BSP proteins may be involved in lipid domain formation and the extraction of some lipids during the sperm maturation process. (C) 2010 Elsevier Inc. All rights reserved.
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