Bovine sperm raft membrane associated Glioma Pathogenesis-Related 1-like protein 1 (GliPr1L1) is modified during the epididymal transit and is potentially involved in sperm binding to the zona pellucida

2012 ◽  
Vol 227 (12) ◽  
pp. 3876-3886 ◽  
Author(s):  
Julieta Caballero ◽  
Gilles Frenette ◽  
Olivier D'Amours ◽  
Clémence Belleannée ◽  
Nicolas Lacroix-Pepin ◽  
...  
Keyword(s):  
Zona Pellucida ◽  
Sperm Binding ◽  
Bovine Sperm ◽  
Pathogenesis Related

Porcine zona pellucida glycoprotein ZP4 is responsible for the sperm-binding activity of the ZP3/ZP4 complex

Zygote ◽  
2011 ◽  
Vol 20 (4) ◽  
pp. 389-397 ◽  
Author(s):  
Naoto Yonezawa ◽  
Saeko Kanai-Kitayama ◽  
Tetsushi Kitayama ◽  
Ayumi Hamano ◽  
Minoru Nakano
Keyword(s):  
Recombinant Proteins ◽  
Zona Pellucida ◽  
Expression System ◽  
Binding Activity ◽  
Carbohydrate Structure ◽  
Mammalian Oocyte ◽  
Sperm Binding ◽  
Bovine Sperm ◽  
Cell Expression ◽  
Cell Expression System

SummaryThe zona pellucida (ZP) is a transparent envelope that surrounds the mammalian oocyte and mediates species-selective sperm–egg interactions. Porcine and bovine ZPs consist of glycoproteins ZP2, ZP3, and ZP4. In both pig and bovine a heterocomplex consisting of ZP3 and ZP4 binds to sperm, however it is not clarified whether ZP3 or ZP4 in the complex is responsible for the sperm binding. Previously, we have established a baculovirus-Sf9 cell expression system for porcine ZP glycoproteins. A mixture of recombinant ZP3 (rZP3) and rZP4 displayed sperm-binding activity toward bovine sperm but not porcine sperm, probably due to differences in carbohydrate structure between the native and recombinant ZP glycoproteins. In this study, a mixture of porcine rZP3 and native ZP4 (nZP4) inhibited the binding of porcine sperm to the ZP. In contrast, a mixture of porcine nZP3 and rZP4 did not inhibit the binding of porcine sperm, although the mixture inhibited the binding of bovine sperm. The porcine rZP3/nZP4 mixture bound to the acrosomal region of porcine sperm, in a manner similar to that of the nZP3/nZP4 mixture. nZP3 was precipitated with rZP4, and nZP4 was precipitated with rZP3 by utilising the N-terminal tags on the recombinant proteins. These results indicated that nZP4, but not rZP4, is necessary for binding activity of porcine ZP3/ZP4 complex towards porcine sperm and further suggested that the carbohydrate structures of ZP4 in the porcine ZP3/ZP4 complex are responsible for porcine sperm-binding activity of the complex.

scholarly journals Sperm-binding regions on bovine egg zona pellucida glycoprotein ZP4 studied in a solid supported form on plastic plate

PLoS ONE ◽  
2021 ◽  
Vol 16 (7) ◽  
pp. e0254234
Author(s):  
Kamila Dilimulati ◽  
Misaki Orita ◽  
Ganbat Undram ◽  
Naoto Yonezawa
Keyword(s):  
Zona Pellucida ◽  
Binding Sites ◽  
Insect Cells ◽  
Competitive Inhibition ◽  
Expression System ◽  
Binding Activity ◽  
Mammalian Oocyte ◽  
Sperm Binding ◽  
Bovine Sperm ◽  
Binding Mechanisms

The zona pellucida (ZP) is a transparent envelope that surrounds the mammalian oocyte and mediates species-selective sperm–oocyte interactions. The bovine ZP consists of the glycoproteins ZP2, ZP3, and ZP4. Sperm-binding mechanisms of the bovine ZP are not yet fully elucidated. In a previous report, we established the expression system of bovine ZP glycoproteins using Sf9 insect cells and found that the ZP3/ZP4 heterocomplex inhibits the binding of sperm to the ZP in a competitive inhibition assay, while ZP2, ZP3, ZP4, the ZP2/ZP3 complex, and the ZP2/ZP4 complex do not exhibit this activity. Here, we show that bovine sperm binds to plastic plates coated with ZP4 in the absence of ZP3. We made a series of ZP4 deletion mutants to study the sperm-binding sites. The N-terminal region, Lys-25 to Asp-136, and the middle region, Ser-290 to Lys-340, of ZP4 exhibit sperm-binding activity. These results suggest that among the three components of bovine ZP glycoproteins, ZP4 contains the major potential sperm-binding sites, and the formation of a multivalent complex is necessary for the sperm-binding activity of ZP4.

Differences between antigenic determinants of pig and cat zona pellucida proteins

Reproduction ◽  
2000 ◽  
pp. 15-23 ◽  
Author(s):  
K Jewgenow ◽  
M Rohleder ◽  
I Wegner
Keyword(s):  
In Vitro Fertilization ◽  
Zona Pellucida ◽  
Antigenic Determinants ◽  
Vitro Fertilization ◽  
Contraceptive Vaccine ◽  
Sperm Binding ◽  
Dependent Inhibition ◽  
Dose Dependent Inhibition ◽  
Dose Dependent

Despite many efforts, the control of reproduction in feral cat populations is still a problem in urban regions around the world. Immunocontraception is a promising approach; thus the present study examined the suitability of the widely used pig zona pellucida proteins (pZP) for contraception in feral domestic cats. Purified zona pellucida proteins obtained from pig and cat ovaries were used to produce highly specific antisera in rabbits. Antibodies against pZP raised in rabbits or lions were not effective inhibitors of either in vitro sperm binding (cat spermatozoa to cat oocytes) or in vitro fertilization in cats, whereas antibodies against feline zona pellucida proteins (fZP) raised in rabbits showed a dose-dependent inhibition of in vitro fertilization. Immunoelectrophoresis, ELISA and immunohistology of ovaries confirmed these results, showing crossreactivity of anti-fZP sera to fZP and to a lesser extent to pZP, but no interaction of anti-pZP sera with fZP. It is concluded that cat and pig zonae pellucidae express a very small number of shared antigenic determinants, making the use of pZP vaccine in cats questionable. A contraceptive vaccine based on feline zona pellucida determinants will be a better choice for the control of reproduction in feral cats if immunogenity can be achieved.

Sperm binding to the human zona pellucida and calcium influx in response to GnRH and progesterone

Andrologia ◽  
2002 ◽  
Vol 34 (5) ◽  
pp. 301-307 ◽  
Author(s):  
P. Morales ◽  
E. Pizarro ◽  
M. Kong ◽  
C. Pasten
Keyword(s):  
Zona Pellucida ◽  
Calcium Influx ◽  
Sperm Binding

scholarly journals Glioma Pathogenesis-Related 1-Like 1 Is Testis Enriched, Dynamically Modified, and Redistributed during Male Germ Cell Maturation and Has a Potential Role in Sperm-Oocyte Binding

Endocrinology ◽  
2010 ◽  
Vol 151 (5) ◽  
pp. 2331-2342 ◽  
Author(s):  
Gerard M. Gibbs ◽  
Jennifer Chi Yi Lo ◽  
Brett Nixon ◽  
Duangporn Jamsai ◽  
Anne E. O'Connor ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Zona Pellucida ◽  
Secretory Protein ◽  
Cellular Adhesion ◽  
Binding Assays ◽  
Distinct Subgroup ◽  
Functional Studies ◽  
Pathogenesis Related ◽  
Antigen 5

The glioma pathogenesis-related 1 (GLIPR1) family consists of three genes [GLIPR1, GLIPR1-like 1 (GLIPR1L1), and GLIPR1-like 2 (GLIPR1L2)] and forms a distinct subgroup within the cysteine-rich secretory protein (CRISP), antigen 5, and pathogenesis-related 1 (CAP) superfamily. CAP superfamily proteins are found in phyla ranging from plants to humans and, based largely on expression and limited functional studies, are hypothesized to have roles in carcinogenesis, immunity, cell adhesion, and male fertility. Specifically data from a number of systems suggests that sequences within the C-terminal CAP domain of CAP proteins have the ability to promote cell-cell adhesion. Herein we cloned mouse Glipr1l1 and have shown it has a testis-enriched expression profile. GLIPR1L1 is posttranslationally modified by N-linked glycosylation during spermatogenesis and ultimately becomes localized to the connecting piece of elongated spermatids and sperm. After sperm capacitation, however, GLIPR1L1 is also localized to the anterior regions of the sperm head. Zona pellucida binding assays indicate that GLIPR1L1 has a role in the binding of sperm to the zona pellucida surrounding the oocyte. These data suggest that, along with other members of the CAP superfamily and several other proteins, GLIPR1L1 is involved in the binding of sperm to the oocyte complex. Collectively these data further strengthen the role of CAP domain-containing proteins in cellular adhesion and propose a mechanism whereby CAP proteins show overlapping functional significance during fertilization.

Characterization of Human Sperm Binding to Homologous Recombinant Zona Pellucida Proteins

2011 ◽  
Vol 18 (9) ◽  
pp. 876-885 ◽  
Author(s):  
Mayel Chirinos ◽  
Cecilia Cariño ◽  
María Elena González-González ◽  
Ernesto Arreola ◽  
Rodrigo Reveles ◽  
...  
Keyword(s):  
Zona Pellucida ◽  
Human Sperm ◽  
Sperm Binding

scholarly journals A single domain of the ZP2 zona pellucida protein mediates gamete recognition in mice and humans

2014 ◽  
Vol 205 (6) ◽  
pp. 801-809 ◽  
Author(s):  
Matteo A. Avella ◽  
Boris Baibakov ◽  
Jurrien Dean
Keyword(s):  
Transgenic Mice ◽  
Zona Pellucida ◽  
Human Sperm ◽  
Recombinant Peptide ◽  
Genetic Ablation ◽  
Sperm Binding ◽  
Gamete Recognition ◽  
Mammalian Fertilization ◽  
Human And Mouse

The extracellular zona pellucida surrounds ovulated eggs and mediates gamete recognition that is essential for mammalian fertilization. Zonae matrices contain three (mouse) or four (human) glycoproteins (ZP1–4), but which protein binds sperm remains controversial. A defining characteristic of an essential zona ligand is sterility after genetic ablation. We have established transgenic mice expressing human ZP4 that form zonae pellucidae in the absence of mouse or human ZP2. Neither mouse nor human sperm bound to these ovulated eggs, and these female mice were sterile after in vivo insemination or natural mating. The same phenotype was observed with truncated ZP2 that lacks a restricted domain within ZP251–149. Chimeric human/mouse ZP2 isoforms expressed in transgenic mice and recombinant peptide bead assays confirmed that this region accounts for the taxon specificity observed in human–mouse gamete recognition. These observations in transgenic mice document that the ZP251–149 sperm-binding domain is necessary for human and mouse gamete recognition and penetration through the zona pellucida.

scholarly journals The molecular basis of mouse sperm–zona pellucida binding: a still unresolved issue in developmental biology

Reproduction ◽  
2011 ◽  
Vol 142 (3) ◽  
pp. 377-381 ◽  
Author(s):  
Gary F Clark
Keyword(s):  
Zona Pellucida ◽  
Molecular Basis ◽  
Three Dimensional ◽  
Inhibitory Effect ◽  
Specific Model ◽  
Cell Stage ◽  
Sperm Binding ◽  
Potent Inhibitory Effect ◽  
Alternate Model ◽  
Sperm Plasma Membrane

During murine fertilization, sperm bind to the specialized extracellular matrix of the egg, known as the zona pellucida (ZP). This matrix is composed of three major glycoproteins designated ZP1, ZP2, and ZP3. Three models for sperm–ZP binding are now under consideration. The domain-specific model posits that adhesion relies primarily on interactions between N-glycans located within the C-terminal domain of ZP3 and a lectin-like egg-binding protein in the sperm plasma membrane. However, this model does not explain recent results obtained in studies with ZP2mut mice. In the supramolecular structure model, sperm bind to a three-dimensional zona matrix that depends on the cleavage status of ZP2. This paradigm does not explain the potent inhibitory effect of specific carbohydrate sequences or a C-terminal glycopeptide (gp55) derived from ZP3. Recently, O-glycans linked at Thr155 and Thr162 of ZP3 were implicated as potential ligands that mediate initial sperm–ZP binding. This novel model will be reviewed. A major challenge is to develop an alternate model for sperm–ZP binding that fits as much of the data as possible. Such a model is presented in this review. This paradigm could explain how the inability to cleave ZP2mut in ZP2mut mice could result in continued sperm binding to two-cell stage embryos without the formation of a supramolecular binding complex. These novel insights should guide future experiments that will eventually determine the molecular basis underlying gamete binding in the mouse and other eutherian mammals.

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