1985
DOI: 10.1016/0092-8674(85)90084-4
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O-linked oligosaccharides of mouse egg ZP3 account for its sperm receptor activity

Abstract: Previously, we reported that ZP3, one of three different glycoproteins present in the mouse egg's zona pellucida, serves as a sperm receptor. Furthermore, small glycopeptides derived from egg ZP3 retain full sperm receptor activity, suggesting a role for carbohydrate, rather than polypeptide chain in receptor function. Here, we report that removal of O-linked oligosaccharides from ZP3 destroys its sperm receptor activity, whereas removal of N-linked oligosaccharides has no effect. A specific size class of O-li… Show more

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Cited by 564 publications
(347 citation statements)
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“…Furthermore, in a diverse range of organisms (from echinoderms to mammals), the recognition of carbohydrate epitopes by complementary protein receptors has been proposed to be a critical factor in gamete interaction [1][2][3].…”
Section: Introductionmentioning
confidence: 99%
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“…Furthermore, in a diverse range of organisms (from echinoderms to mammals), the recognition of carbohydrate epitopes by complementary protein receptors has been proposed to be a critical factor in gamete interaction [1][2][3].…”
Section: Introductionmentioning
confidence: 99%
“…In mammals such as mice and pigs, it is generally accepted that carbohydrate epitopes displayed by zona pellucida glycoprotein 3 (ZP3) play a pivotal role in spermatozoa-ZP3 interaction [2,7]. However, although both native human zona pellucida and purified, glycosylated recombinant human ZP3 (rhuZP3) secreted by Chinese Hamster Ovary (CHO) cells have been shown to stimulate acrosomal exocytosis in human spermatozoa [8][9][10][11], it has yet to be firmly established whether the ability Abbreviations used : IPTG, isopropyl-β-D-thiogalactopyranoside ; OD 595 , optical density at 595 nm ; rhuZP3, recombinant human ZP3 ; GST-HuZP3, glutathione S-transferase-recombinant human ZP3 fusion protein ; TTB, Towbin Transfer Buffer.…”
Section: Introductionmentioning
confidence: 99%
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“…However, selective removal of N-linked oligosaccharides from mouse ZP3 by endo-b-N-acetyl-D-glucosamine treatment has no effect on the induction of the AR, whereas removal of O-linked oligosaccharides by alkaline hydrolysis abrogates its ability to induce the AR. 90 Initial studies implicated galactose in a-or b-linkages at the non-reducing terminus of O-linked oligosaccharides and N-acetylglucosamine (GlcNAc) in b-linkages as the sugar determinants on mouse ZP3 that are responsible for the binding of sperm to the ZP. 91 However, mice deficient in glycosyl transferase, which amends terminal galactose in an a-linkage, are fully fertile 92,93 implicating galactose in b-linkages or GlcNAc or both as critical residues.…”
Section: Zp4mentioning
confidence: 99%