Abstract
Methods are described that have been used for characterizing the interaction of the soluble bovine seminal plasma protein PDC-109 with liposomes. PDC-109 binds to bull sperm cells upon ejaculation and is an important modulating factor of sperm cell maturation. The binding of the protein to sperm cells is mediated via lipids of the sperm plasma membrane. Most of our current knowledge about the molecular mechanisms of PDC-109-membrane interaction has been obtained by studies employing lipid vesicles. The experimental strategy described here can be applied to investigate the interaction of soluble proteins with membranes in order to understand their physiological role.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Similar content being viewed by others
References
Winget JM, Pan YH, Bahnson BJ (2006) The interfacial binding surface of phospholipase A2s: PLA2. Biochim Biophys Acta 1761:1260-1269
Waisman DM (1995) Annexin II tetramer: structure and function. Mol Cell Biochem 150:301-322
Cabiaux V, Wolff C, Ruysschaert JM (1997) Interaction with a lipid membrane: a key step in bacterial toxins virulence. Int J Biol Macromol 21:285-298
Palmer M (2004) Cholesterol and the activity of bacterial toxins. FEMS Microbiol Lett 238:281-289
Davidson WS, Jonas A, Clayton DF, George JM (1998) Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes. J Biol Chem 273:9443-9449
Beyer K (2007) Mechanistic aspects of Parkinson’s disease: alpha-synuclein and the biomembrane. Cell Biochem Biophys 47:285-299
Skorstengaard K, Thogersen HC, Petersen TE (1984) Complete primary structure of the collagen-binding domain of bovine fibronectin. Eur J Biochem 140:235-243
Manjunath P, Sairam MR (1987) Purification and biochemical characterization of three major acidic proteins (BSP-A1, BSP-A2 and BSP-A3) from bovine seminal plasma. Biochem J 241:685-692
Therien I, Bleau G, Manjunath P (1995) Phosphatidylcholine-binding proteins of bovine seminal plasma modulate capacitation of spermatozoa by heparin. Biol Reprod 52:1372-1379
Wah DA, Fernández-Tornero C, Sanz L, Romero A, Calvete JJ (2002) Sperm coating mechanism from the 1.8 A crystal structure of PDC-109-phosphorylcholine complex. Structure 10:505-514
Manjunath P, Therien I (2002) Role of seminal plasma phospholipid-binding proteins in sperm membrane lipid modification that occurs during capacitation. J Reprod Immunol 53:109-119
Ekhlasi-Hundrieser M, Müller P, Töpfer-Petersen E (2008) Male secretory proteins sperm tools for fertilisation. In: Glander HJ, Paasch U (eds) Biology of male germ cells. Shaker Publisher GmbH, Aachen, Germany
Calvete JJ, Varela PF, Sanz L, Romero A, Mann K, Töpfer-Petersen E (1996) A procedure for the large-scale isolation of bovine seminal plasma proteins. Protein Expr Purif 8:48-56
Fellmann P, Zachowski A, Devaux PF (1994) Synthesis and use of spin-labeled lipids for studies of the transmembrane movement of phospholipids. Methods Mol Biol 27:161-175
Mayer LD, Hope MJ, Cullis RP, Janoff AS (1985) Solute distributions and trapping efficiencies observed in freeze-thawed multilamellar vesicles. Biochim Biophys Acta 817:193-196
Heuer K, Arbuzova A, Strauss H, Kofler M, Freund C (2005) The helically extended SH3 domain of the T cell adaptor protein ADAP is a novel lipid interaction domain. J Mol Biol 348:1025-1035
Buser CA, McLaughlin S (1998) Ultracentri-fugation technique for measuring the binding of peptides and proteins to sucrose-loaded phospholipid vesicles. Methods Mol Biol 84:267-281
Bigay J, Casella JF, Drin G, Mesmin B, Antonny B (2005) ArfGAP1 responds to membrane curvature through the folding of a lipid packing sensor motif. EMBO J 24:2244-2253
Desnoyers L, Manjunath P (1992) Major proteins of bovine seminal plasma exhibit novel interactions with phospholipid. J Biol Chem 267:10149-10155
Müller P, Erlemann KR, Müller K, Calvete JJ, Töpfer-Petersen E, Marienfeld K, Herrmann A (1998) Biophysical characterization of the interaction of bovine seminal plasma protein PDC-109 with phospholipid vesicles. Eur Biophys J 27:33-41
Marsh D, Horvath LI (1998) Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling. Biochim Biophys Acta 1376:267-296
Greube A, Müller K, Töpfer-Petersen E, Herrmann A, Müller P (2001) Influence of the bovine seminal plasma protein PDC-109 on the physical state of membranes. Biochemistry 40:8326-8334
Tannert A, Töpfer-Petersen E, Herrmann A, Müller K, Müller P (2007) The lipid composition modulates the influence of the bovine seminal plasma protein PDC-109 on membrane stability. Biochemistry 46:11621-11629
Greube A, Müller K, Töpfer-Petersen E, Herrmann A, Müller P (2004) Interaction of fibronectin type II proteins with membranes: the stallion seminal plasma protein SP-1/2. Biochemistry 43:464-472
Müller P, Greube A, Töpfer-Petersen E, Herrmann A (2002) Influence of the bovine seminal plasma protein PDC-109 on cholesterol in the presence of phospholipids. Eur Biophys J 31:438-447
Acknowledgments
The work was supported by the Deutsche Forschungsgemeinschaft (Mu 1017/2). The fruitful cooperation during this project with Edda Töpfer-Petersen is kindly acknowledged. We thank Anja Arbuzova for critical reading of the manuscript.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2010 Humana Press, a part of Springer Science+Business Media, LLC
About this protocol
Cite this protocol
Höfer, C.T., Herrmann, A., Müller, P. (2010). Use of Liposomes for Studying Interactions of Soluble Proteins with Cellular Membranes. In: Weissig, V. (eds) Liposomes. Methods in Molecular Biology™, vol 606. Humana Press. https://doi.org/10.1007/978-1-60761-447-0_6
Download citation
DOI: https://doi.org/10.1007/978-1-60761-447-0_6
Published:
Publisher Name: Humana Press
Print ISBN: 978-1-60761-446-3
Online ISBN: 978-1-60761-447-0
eBook Packages: Springer Protocols