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Science 5 March 1993:
Vol. 259. no. 5100, pp. 1421 - 1425
DOI: 10.1126/science.8383878
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Articles

Science, Vol 259, Issue 5100, 1421-1425
Copyright © 1993 by American Association for the Advancement of Science

articles

Sea urchin egg receptor for sperm: sequence similarity of binding domain and hsp70

KR Foltz, JS Partin, and WJ Lennarz

Department of Biological Sciences, University of California, Santa Barbara 93106.

Fertilization depends on cell surface recognition proteins that interact and thereby mediate binding and subsequent fusion of the sperm and egg. Overlapping complementary DNA's encoding the egg plasma membrane receptor for sperm from the sea urchin Strongylocentrotus purpuratus were cloned and sequenced. Analysis of the deduced primary structure suggests that the receptor is a transmembrane protein with a short cytoplasmic domain. This domain showed no sequence similarity to known protein sequences. In contrast, the extracellular, sperm binding domain of the receptor did show sequence similarity to the heat shock protein 70 (hsp70) family of proteins. Recombinant protein representing this portion of the receptor bound to the sperm protein, binding, and also inhibited fertilization in a species-specific manner; beads coated with the protein became specifically bound to acrosome-reacted sperm. These data provide a basis for detailed investigations of molecular interactions that occur in gamete recognition and egg activation.


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Identification of the Sea Urchin 350-kDa Sperm-binding Protein as a New Sialic Acid-binding Lectin That Belongs to the Heat Shock Protein 110 Family: IMPLICATION OF ITS BINDING TO GANGLIOSIDES IN SPERM LIPID RAFTS IN FERTILIZATION.
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Surface Accessibility of the 70-Kilodalton Chlamydia trachomatis Heat Shock Protein following Reduction of Outer Membrane Protein Disulfide Bonds.
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The Chaperoning Activity of hsp110. IDENTIFICATION OF FUNCTIONAL DOMAINS BY USE OF TARGETED DELETIONS.
H. J. Oh, D. Easton, M. Murawski, Y. Kaneko, and J. R. Subjeck (1999)
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Characterization of an Acidic-pH-Inducible Stress Protein (hsp70), a Putative Sulfatide Binding Adhesin, from Helicobacter pylori.
M. Huesca, A. Goodwin, A. Bhagwansingh, P. Hoffman, and C. A. Lingwood (1998)
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Characterization of the Hsp110/SSE gene family response to hyperosmolality and other stresses.
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Am J Physiol Renal Physiol 274, F1054-F1061
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Identification of sulfated oligosialic acid units in the O-linked glycan of the sea urchin egg receptor for sperm.
S. Kitazume-Kawaguchi, S. Inoue, Y. Inoue, and W. J. Lennarz (1997)
PNAS 94, 3650-3655
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Gamete Interactions in Xenopus laevis: Identification of Sperm Binding Glycoproteins in the Egg Vitelline Envelope.
J. Tian, H. Gong, G. H. Thomsen, and W. J. Lennarz (1997)
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Purification and Characterization of a Src-related p57 Protein-tyrosine Kinase from Xenopus Oocytes. ISOLATION OF AN INACTIVE FORM OF THE ENZYME AND ITS ACTIVATION AND TRANSLOCATION UPON FERTILIZATION.
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Osmotic Stress Protein 94 (Osp94).
R. Kojima, J. Randall, B. M. Brenner, and S. R. Gullans (1996)
J. Biol. Chem. 271, 12327-12332
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The Occurrence of Novel 9-O-Sulfated N-Glycolylneuraminic Acid-capped alpha2[IMAGE]5-O[IMAGE]-linked Oligo/PolyNeu5Gc Chains in Sea Urchin Egg Cell Surface Glycoprotein.
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J. Biol. Chem. 271, 6694-6701
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Cloning and Expression of Murine High Molecular Mass Heat Shock Proteins, HSP105.
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Identification of a Major Subfamily of Large hsp70-like Proteins through the Cloning of the Mammalian 110-kDa Heat Shock Protein.
D. Lee-Yoon, D. Easton, M. Murawski, R. Burd, and J. R. Subjeck (1995)
J. Biol. Chem. 270, 15725-15733
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The ATPase Domain of hsp70 Possesses a Unique Binding Specificity for 3'-Sulfogalactolipids.
D. Mamelak and C. Lingwood (2001)
J. Biol. Chem. 276, 449-456
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