High impact information on ZP2

• The zona pellucida, which surrounds the mammalian oocyte, consists of the ZPA, ZPB, and ZPC glycoproteins and plays roles in species-selective sperm-egg interactions via its carbohydrate moieties [1].
• Results of experiments presented suggest the following: (1) sperm bind specifically to ZP3-beads, but not to silica beads either exposed to 2-aminoethanol or derivatized with oocyte ZP2, fetuin or bovine serum albumin [2].
• In this study, we have mapped and characterized a B cell epitope of sulfated glycoprotein ZP2 (ZP2) as a step toward the development of a multi-epitope zona pellucida (ZP) vaccine [3].
• A chimeric peptide was constructed that contained the YRYK motif of ZP2 and a bovine RNase T cell epitope [3].
• When normal or ovariectomized female mice were immunized with three overlapping peptides that span this region of ZP2 (101-120, 111-130, 121-140), only ZP2(121-140) elicited IgG antibodies that reacted with mouse ovarian ZP, indicative of the presence of native B epitope and helper T cell epitope in ZP2(121-140) [3].

Biological context of ZP2

• In this study, we deduced amino-acid sequences of bovine ZPA and ZPB by cDNA cloning and sequencing [4].

Anatomical context of ZP2

• To more finely map the ZP2 B cell epitope, a random peptide display library was screened with the IE-3 antibody, and a consensus tetramer sequence VxYK that matched the ZP2(123-126) sequence VRYK was located [3].
• The objective of these studies was to identify ZP2 and ZP3 domains that may be of importance for the induction of the acrosome reaction [5].

Associations of ZP2 with chemical compounds

• Localization of N-linked carbohydrate chains in glycoprotein ZPA of the bovine egg zona pellucida [6].
• Bovine ZPA was processed between Ala and Asp on fertilization, suggesting that the consensus motif for the processing is Ala-Asp-Asp/Glu [4].
• Acidic complex-type chains were found at all three N-glycosylation sites, while Man5GlcNAc2 was found at Asn83 and Asn191, but there was very little of this sperm-ligand active chain at Asn527 in the ZP domain of ZPA [6].
• The positions of Cys were completely conserved in bovine ZPA and ZPB compared with counterparts of other mammalian species [4].

Analytical, diagnostic and therapeutic context of ZP2

• Molecular cloning of bovine zona pellucida glycoproteins ZPA and ZPB and analysis for sperm-binding component of the zona [4].

References