Conversion of Ser to Thr residues at the sperm combining-site of mZP3 does not affect sperm receptor activity

Biochemical and Biophysical Research Communications

Volumn 301, Issue 4, 2003, Pages 813-818

  Williams, Zev ^a   Litscher, Eveline S ^a   Wassarman, Paul M ^a  

^a MOUNT SINAI SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEIN; RECOMBINANT PROTEIN; SERINE; THREONINE;

ANIMAL CELL; ARTICLE; BINDING AFFINITY; CELL ASSAY; CONTROLLED STUDY; EGG; FEMALE; GENETIC TRANSFECTION; IN VITRO STUDY; MALE; MOUSE; NONHUMAN; OVULATION; PRIORITY JOURNAL; PROTEIN FUNCTION; PURIFICATION; SITE DIRECTED MUTAGENESIS; SPERM;

MAMMALIA;

EID: 0037458978     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(03)00044-5     Document Type: Article

References (37)

1. Varki A., Cummings R., Esko J., Freeze H., Hart G., Marth J. Essentials of Glycobiology. 1999;Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
2. Ha S.J., Chang J., Song M.K., Suh Y.S., Jin H.T., Lee C.H., Nam G.H., Choi G., Choi K.Y., Lee S.H.et al. Engineering N-glycosylation mutations in IL-12 enhances sustained cytotoxic T lymphocyte responses for DNA immunization. Nat. Biotechnol. 20:2002;381-386.
3. Elhammer A.P., Kezdy F.G., Kurosaka A. The acceptor specificity of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases. Glycoconj. J. 16:1999;171-180.
4. O'Connell B.C., Hagen F.K., Tabak L.A. The influence of flanking sequence on the O-glycosylation of threonine in vitro. J. Biol. Chem. 267:1992;25010-25018.
5. Wang Y., Abernethy J.L., Eckhardt A.E., Hill R.L. Purification and characterization of a UDP-GalNAc:polypeptide N-acetylgalactosaminyl-transferase specific for glycosylation of threonine residues. J. Biol. Chem. 267:1992;12709-12716.
6. Elhammer A.P., Poorman R.A., Brown E., Maggiora L.L., Hoogerheide J.G., Kezdy F.G. The specificity of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase as inferrred from a database of in vivo substrates and from the in vitro glycosylation of proteins and peptides. J. Biol. Chem. 14:1993;10029-10038.
7. Nehrke K., Hagen F.K., Tabak L.A. Charge distribution of flanking amino acids influences O-glycan acquisition in vivo. J. Biol. Chem. 271:1996;7061-7065.
8. O'Connell B., Tabak L.A., Ramasubbu N. The influence of flanking sequences on O-glycosylation. Biochem. Biophys. Res. Commun. 180:1991;1024-1030.
9. Hansen J.E., Lund O., Engelbrecht J., Bohr H., Nielsen J.O., Hansen J.E. Prediction of O-glycosylation of mammalian proteins: specificity patterns of UDP-GalNAc:polypeptide N-acteylgalactosaminyltransferase. Biochem. J. 308:1995;801-813.
10. Wassarman P.M. Zona pellucida glycoproteins. Annu. Rev. Biochem. 57:1988;415-442.
11. Wassarman P.M. Mammalian fertilization: molecular aspects of gamete adhesion. Cell. 96:1999;175-183.
12. Wassarman P.M., Jovine L., Litscher E.S. A profile of fertilization in mammals. Nat. Cell Biol. 3:2001;E59-E64.
13. Jovine L., Litscher E.S., Wassarman P.M. Egg zona pellucida, egg vitelline envelope, and related extracellular glycoproteins. Adv. Dev. Biol. Biochem. 12:2002;31-54.
14. Kinloch R.A., Mortillo S., Stewart C.L., Wassarman P.M. Embryonal carcinoma cells transfected with ZP3 genes differentially glycosylate similar polypeptides and secrete active mouse sperm receptor. J. Cell Biol. 115:1991;655-664.
15. Chen J., Litscher E.S., Wassarman P.M. Inactivation of the mouse sperm receptor, mZP3, by site-directed mutagenesis of individual serine residues located at the combining site for sperm. Proc. Natl. Acad. Sci. USA. 95:1998;6193-6197.
16. Litscher E.S., Juntunen K., Seppo A., Penttila L., Niemela R., Renkonen O., Wassarman P.M. Oligosaccharide constructs with defined structures that inhibit binding of mouse sperm to unfertilized eggs in vitro. Biochemistry. 34:1995;4662-4669.
17. Johnston D.S., Wright W.W., Shaper J.H., Hokke C.H., Van den Eijnden D.H., Joziasse D.H. Murine sperm-zona binding, a fucosyl residue is required for high affinity sperm-binding ligand. A second site on sperm binds a nonfucosylated, β-galactosyl-capped oligosaccharide. J. Biol. Chem. 273:1998;1888-1895.
18. Kinloch R.A., Sakai Y., Wassarman P.M. Mapping the mouse ZP3 combining site for sperm by exon swapping and site-directed mutagenesis. Proc. Natl. Acad. Sci. USA. 92:1995;263-267.
19. Bleil J.D., Wassarman P.M. Autoradiographic visualization of the mouse egg's sperm receptor bound to sperm. J. Cell Biol. 102:1986;1363-1371.
20. Moller C.C., Bleil J.D., Kinloch R.A., Wassarman P.M. Structural and functional relationships between mouse and hamster zona pellucida glycoproteins. Dev. Biol. 137:1990;276-286.
21. Litscher E.S., Wassarman P.M. Recombinant hamster sperm receptors that exhibit species-specific binding to sperm. Zygote. 4:1996;229-236.
22. Bork P., Sander C. A large domain common to sperm receptors (Zp2 and Zp3) and TGF-β type III receptor. FEBS Lett. 300:1992;237-240.
23. Jovine L., Qi H., Williams Z., Litscher E., Wassarman P.M. The ZP domain is a conserved module for protein polymerization. Nat. Cell Biol. 4:2000;457-461.
24. Litscher E.S., Qi H., Wassarman P.M. Mouse zona pellucida glycoproteins mZP2 and mZP3 undergo carboxy-terminal proteolytic processing in growing oocytes. Biochemistry. 38:1999;12280-12287.
25. Williams Z., Wassarman P.M. Secretion of mouse ZP3, the sperm receptor, requires cleavage of its polypeptide at a consensus furin cleavage site. Biochemistry. 40:2001;929-937.
26. Kiefer S.M., Saling P. Proteolytic processing of human zona pellucida proteins. Biol. Reprod. 66:2002;407-414.
27. Bleil J.D., Wassarman P.M. Mammalian sperm-egg interaction: identification of a glycoprotein in mouse egg zonae pellucidae possessing receptor activity for sperm. Cell. 20:1980;873-882.
28. Schwientek T., Yeh J.C., Levery S.B., Keck B., Merkx G., van Kessel A.G., Fukuda M., Clausen H. Control of O-glycan branch formation. J. Biol. Chem. 275:2000;11106-11113.
29. Davis B.G. Synthesis of glycoproteins. Chem. Rev. 102:2002;579-601.
30. Weitzman S., Grennon M. Comparison of Sinbus virus and immunoglobulin glycopeptides in mouse myeloma cells. J. Biol. Chem. 254:1979;5377-5382.
31. Hart G.W., Dahms N.M. Influence of quaternary structure on glycosylation. J. Biol. Chem. 261:1986;13186-13196.
32. Nehrke K., Ten-Hagen K.G., Hagen F.K., Tabak L.A. Charge distribution of flanking amino acids inhibits O-glycosylation of several single-site acceptors in vivo. Glycobiology. 8:1997;1053-1060.
33. Kato K., Takeuchi H., Kanoh A., Mandel U., Hassan H., Clausen H., Irimura T. N-acetylgalactosamine incorporation into a peptide containing consecutive threonine residues by UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactos-aminyltransferases. Glycobiology. 11:2001;821-829.
34. Kato K., Takeuchi H., Miyahara N., Kanoh A., Hassan H., Clausen H., Irimura T. Distinct orders of GalNAc incorporation into a peptide with consecutive threonines. Biochem. Biophys. Res. Commun. 287:2001;110-115.
35. Wassarman P.M., Litscher E.S. Sperm-egg recognition mechanisms in mammals. Curr. Topics Dev. Biol. 30:1995;1-19.
36. Swanson W.J., Yang Z., Wolfner M.F., Aquadro C.F. Positive Darwinian selection drives the evolution of several female reproductive proteins in mammals. Proc. Natl. Acad. Sci. USA. 98:2001;2509-2514.
37. Florman H.M., Wassarman P.M. O-linked oligosaccharides of mouse egg ZP3 account for its sperm receptor activity. Cell. 41:1985;313-324.