scholarly journals Characterization of a novel ZP3-independent sperm-binding ligand that facilitates sperm adhesion to the egg coat

Development ◽  
2004 ◽  
Vol 131 (3) ◽  
pp. 503-512 ◽  
Author(s):  
C. Rodeheffer
Keyword(s):  
Sperm Binding ◽  
Egg Coat

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

Structural and molecular characterization of equine sperm-binding fibronectin-II module proteins

2004 ◽  
Vol 70 (1) ◽  
pp. 45-57 ◽  
Author(s):  
Mahnaz Ekhlasi-Hundrieser ◽  
Bettina Schäfer ◽  
Christiane Kirchhoff ◽  
Oliver Hess ◽  
Simone Bellair ◽  
...  
Keyword(s):  
Molecular Characterization ◽  
Sperm Binding

scholarly journals Kinetic characterization of the changes in protein tyrosine phosphorylation of membranes, cytosolic Ca2+ concentration and viability in boar sperm populations selected by binding to oviductal epithelial cells

Reproduction ◽  
2001 ◽  
pp. 469-480 ◽  
Author(s):  
AM Petrunkina ◽  
J Friedrich ◽  
W Drommer ◽  
G Bicker ◽  
D Waberski ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Tyrosine Phosphorylation ◽  
Membrane Integrity ◽  
Free Swimming ◽  
Sperm Binding ◽  
Preferential Binding ◽  
Functional Modulation ◽  
And Control ◽  
Boar Spermatozoa

On reaching the oviduct, spermatozoa are retained in the isthmic region of the oviduct until ovulation occurs. The essential steps of capacitation are co-ordinated in this region. In this study, a primary cell culture system of oviductal epithelial cells was established to investigate sperm binding to oviductal epithelium and modulation of sperm function during incubation under capacitating conditions in co-culture with oviductal epithelial cells. Epithelial cells were stripped from the oviducts of sows and cultivated for 5-7 days on Lab-Tek Chamber slides on Matrigel. The preparations on chamber slides and suspensions of control spermatozoa were incubated for 3 h in Tyrode's albumin lactate pyruvate (TALP) medium. At 3, 30, 60, 90 and 180 min the free-swimming spermatozoa were collected by washing, and membrane integrity, tyrosine phosphorylation patterns and [Ca(2+)](i) of bound, unbound and control spermatozoa were assessed with fluorescent probes (propidium iodide, Cy-3 and fluo-3-AM). The cells bound to oviductal epithelial cells showed reduced cytosolic Ca(2+) concentration, reduced and almost absent tyrosine phosphorylation of membrane proteins and higher viability at the time of the first sampling. Increases in Ca(2+) concentration and cell death occurred much more slowly during incubation in cells bound to oviductal epithelial cells compared with free-swimming spermatozoa, and no changes in tyrosine phosphorylation were observed. The preferential binding of viable, low-Ca(2+) cells with suppressed tyrosine phosphorylation and slower functional modulation of boar spermatozoa attached to oviductal epithelial cells might represent a mechanism for selecting functionally competent spermatozoa and prolonging their lifespan by delaying capacitation in the oviductal reservoir.

scholarly journals Identification and preliminary characterization of a sperm-binding protein in normal human semen

Reproduction ◽  
1985 ◽  
Vol 73 (1) ◽  
pp. 71-77 ◽  
Author(s):  
P. Abrescia ◽  
G. Lombardi ◽  
M. De Rosa ◽  
L. Quagliozzi ◽  
J. Guardiola ◽  
...  
Keyword(s):  
Binding Protein ◽  
Human Semen ◽  
Preliminary Characterization ◽  
Sperm Binding ◽  
Normal Human

Spermatozoa of the old endemic rodents of Australia – the possible functional significance of their ventral processes

2014 ◽  
Vol 26 (8) ◽  
pp. 1183 ◽  
Author(s):  
Simon Drew ◽  
Chris Leigh ◽  
William G. Breed
Keyword(s):  
Cell Membrane ◽  
Functional Significance ◽  
In Vitro Study ◽  
Cytoskeletal Proteins ◽  
Sperm Transport ◽  
Apical Hook ◽  
Sperm Binding ◽  
Initial Penetration ◽  
Egg Coat

Spermatozoa of the plains mouse (Pseudomys australis), like those of most Australian old endemic rodents, contain, in addition to an apical hook, two further processes that extend from the upper concave surface of the head, the ventral processes. This study shows that these processes contain thiol-rich cytoskeletal proteins, which presumably help to maintain their rigidity during sperm transport, together with the overlying cell membrane having abundant intramembranous proteins. To determine the possible functional significance of these processes, an in vitro study of spermatozoon–zona binding was undertaken. The findings suggest that initial sperm binding occurs by way of the cell membrane over the acrosome of the apical hook and that, subsequently, the lateral surfaces of the ventral processes also become tightly bound to the zona matrix. These ventral processes may therefore have evolved to increase sperm adhesion to the outer zona surface and/or to enhance stabilisation of the spermatozoon at the time of zona binding and initial penetration of the egg coat.

scholarly journals Molecular basis of egg coat cross-linking sheds light on ZP1-associated female infertility

2019 ◽  
Author(s):  
Kaoru Nishimura ◽  
Elisa Dioguardi ◽  
Shunsuke Nishio ◽  
Alessandra Villa ◽  
Ling Han ◽  
...  
Keyword(s):  
Hormonal Contraception ◽  
Cross Linking ◽  
Promising Target ◽  
Domain Of Unknown Function ◽  
Function Characterization ◽  
Cross Links ◽  
Mammalian Fertilization ◽  
Infertile Patients ◽  
Egg Coat

AbstractInteraction between sperm and the egg zona pellucida (ZP) is the first step of mammalian fertilization, and ZP component ZP1 is important for fertility by covalently cross-linking ZP filaments into a matrix. Like ZP4, a structurally-related subunit absent in the mouse, ZP1 is predicted to contain an N-terminal ZP-N domain of unknown function. Characterization of ZP1 proteins carrying mutations from infertile patients suggests that, unlike in the mouse, filament cross-linking by ZP1 is crucial for human ZP assembly. We map the function of ZP1 to its ZP-N1 domain and determine crystal structures of ZP-N1 homodimers from a chicken homolog of ZP1. These reveal that ZP filament cross-linking is highly plastic and can be modulated by ZP1 fucosylation and, potentially, zinc sparks. Moreover, we show that ZP4 ZP-N1 forms non-covalent homodimers in chicken but not human. Together, these data identify human ZP1 cross-links as a promising target for non-hormonal contraception.

scholarly journals Identification of Sperm-Binding Sites in the N-Terminal Domain of Bovine Egg Coat Glycoprotein ZP4

2022 ◽  
Vol 23 (2) ◽  
pp. 762
Author(s):  
Kamila Dilimulati ◽  
Misaki Orita ◽  
Yoshiki Yonahara ◽  
Fabiana Lica Imai ◽  
Naoto Yonezawa
Keyword(s):  
Binding Sites ◽  
Binding Activity ◽  
Binding Region ◽  
Terminal Domain ◽  
Sperm Binding ◽  
Bovine Sperm ◽  
Selective Interaction ◽  
Egg Coat

The species-selective interaction between sperm and egg at the beginning of mammalian fertilisation is partly mediated by a transparent envelope called the zona pellucida (ZP). The ZP is composed of three or four glycoproteins (ZP1–ZP4). The functions of the three proteins present in mice (ZP1–ZP3) have been extensively studied. However, the biological role of ZP4, which was found in all other mammals studied so far, has remained largely unknown. Previously, by developing a solid support assay system, we showed that ZP4 exhibits sperm-binding activity in bovines and the N-terminal domain of bovine ZP4 (bZP4 ZP-N1 domain) is a sperm-binding region. Here, we show that bovine sperm bind to the bZP4 ZP-N1 domain in a species-selective manner and that N-glycosylation is not required for sperm-binding activity. Moreover, we identified three sites involved in sperm binding (site I: from Gln-41 to Pro-46, site II: from Leu-65 to Ser-68 and site III: from Thr-108 to Ile-123) in the bZP4 ZP-N1 domain using chimeric bovine/porcine and bovine/human ZP4 recombinant proteins. These results provide in vitro experimental evidence for the role of the bZP4 ZP-N1 domain in mediating sperm binding to the ZP.

The egg coat zona pellucida 3 glycoprotein – evolution of its putative sperm-binding region in Old World murine rodents (Rodentia: Muridae)

2017 ◽  
Vol 29 (12) ◽  
pp. 2376 ◽  
Author(s):  
Christine A. Swann ◽  
Steven J. B. Cooper ◽  
William G. Breed
Keyword(s):  
Sexual Selection ◽  
Zona Pellucida ◽  
Laboratory Mouse ◽  
Sequence Divergence ◽  
Tail Length ◽  
Good Evidence ◽  
Sperm Binding ◽  
Molecular Divergence ◽  
Murine Rodents ◽  
Egg Coat

In eutherian mammals, before fertilisation can occur the spermatozoon has to bind to, and penetrate, the egg coat, the zona pellucida (ZP). In the laboratory mouse there is good evidence that the primary sperm-binding site is a protein region encoded by Exon 7 of the ZP3 gene and it has been proposed that binding is species specific and evolves by sexual selection. In the present study we investigate these hypotheses by comparing Exon 6 and 7 sequences of ZP3 in 28 species of murine rodents of eight different divisions from Asia, Africa and Australasia, in which a diverse array of sperm morphologies occurs. We found considerable nucleotide (and corresponding amino acid) sequence divergence in Exon 7, but not in Exon 6, across these species, with evidence for positive selection at five codon positions. This molecular divergence does not appear to be due to reinforcement to reduce hybridisation, nor does it correlate with divergence in sperm head morphology or tail length, thus it is unlikely to be driven by inter-male sperm competition. Other forms of post-copulatory sexual selection therefore appear to have resulted in the molecular divergence of this region of ZP3 in this highly speciose group of mammals.

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