Hemizona assay for measuring zona binding in the lowland gorilla

Lanzendorf, Susan E.; Holmgren, W. J.; Johnson, D.; Scobey, M. Joseph; Jeyendran, Rajasingam S.

doi:10.1002/mrd.1080310407

Cited by 22 publications

(18 citation statements)

References 15 publications

(11 reference statements)

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“…Others have shown that human sperm can bind to and penetrate the zona of gibbon and gorilla oocytes, the only exceptions for the human male gamete other than its homologous zona pellucida (Bedford, 1977;Yanagimachi, 1988;Liu et al, 1991;Lanzendorf et al, 1992). On the other hand, it has been shown that gorilla, marmoset and horse sperm can bind to the zona pellucida of salt-stored human oocytes (Liu et al, 1991;Lanzendorf et al, 1992). Here, we have not observed binding of cynomolgus monkey sperm to the human zona pellucida.…”

Section: Discussioncontrasting

confidence: 63%

“…Cynomolgus monkey sperm had a very low binding affinity to the human zona, although they showed a slightly higher rate of acrosome reactions on the heterologous (human) zonae. Others have shown that human sperm can bind to and penetrate the zona of gibbon and gorilla oocytes, the only exceptions for the human male gamete other than its homologous zona pellucida (Bedford, 1977;Yanagimachi, 1988;Liu et al, 1991;Lanzendorf et al, 1992). On the other hand, it has been shown that gorilla, marmoset and horse sperm can bind to the zona pellucida of salt-stored human oocytes (Liu et al, 1991;Lanzendorf et al, 1992).…”

Section: Discussionmentioning

confidence: 99%

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The specificity of human spermatozoa/zona pellucida interaction under hemizona assay conditions

Oehninger

Mahony

Swanson

et al. 1993

Molecular Reproduction Devel

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The objective of this prospective study was to evaluate the specificity of human sperm/zona pellucida interaction under hemizona assay (HZA) conditions in experiments with gametes from the same and different species. Human, cynomolgus monkey and hamster oocytes were used after salt-storage. Oocytes were bisected into matching hemizonae by micromanipulation and used in the HZA. Semen was obtained from healthy men (donors) and male cynomolgus monkeys and prepared by wash and swim-up. Sperm binding to matching hemizonae was assessed (tight binding) after 4-h coincubation in the HZA in homologous and interspecies experiments. Acrosome reaction was evaluated in the sperm droplets using FITC-PSA and on the hemizonae using the T-6 monoclonal antibody. On human hemizonae, the number of tightly bound sperm for human and monkey were 93.2 +/- 15.8 and 3.9 +/- 1.3, respectively (P < 0.001). On monkey hemizonae, the number of tightly bound sperm for monkey and human were 126.0 +/- 34.8 and 2.8 +/- 1.6, (P = 0.02) respectively. On hamster hemizonae, there was negligible binding of human and monkey sperm. There was a significantly higher incidence of acrosome reacted sperm on the zona pellucida in homologous compared to heterologous experiments. These results demonstrate a high species-specificity of human gamete functions under HZA conditions, providing further support for the use of this bioassay in infertility and contraception testing.

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Section: Discussioncontrasting

confidence: 63%

Section: Discussionmentioning

confidence: 99%

The specificity of human spermatozoa/zona pellucida interaction under hemizona assay conditions

Oehninger

Mahony

Swanson

et al. 1993

Molecular Reproduction Devel

View full text Add to dashboard Cite

show abstract

“…Other examples of non‐species‐specific gamete binding and penetration have been observed previously using different combinations of mammalian sperm and oocytes (Bedford, 1977; Yoshimatsu et al, 1988; Liu et al, 1991; Cox, 1992; Lanzendorf et al, 1992; Oehninger et al, 1993).…”

Section: Discussionsupporting

confidence: 60%

First Steps in the Development of a Functional Assay for Human Sperm Using Pig Oocytes

Cánovas

Coy

Gómez

2007

Journal of Andrology

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The use of mammalian oocytes to assess human sperm functionality could be a helpful tool with potential applications in clinical and research programs. In an attempt to develop the pig model, the aim of the present work was to study the interaction between human spermatozoa and pig oocytes at the zona pellucida (ZP), the oolemma, and the ooplasm levels. In vitro matured pig oocytes and human spermatozoa from fertile and low-fertility donors were employed. The induction of the acrosome reaction by the ZP, the ability of the sperm to penetrate the oocyte after cocincubation, and the male pronuclear formation after ICSI were evaluated. Human spermatozoa can bind to pig ZP and undergo the acrosome reaction (15% to 58%, depending on the individual); they are not able to fuse with the oolemma but they can decondense and form a male pronucleus (40%-100%) when injected into pig oocytes. In conclusion, this study shows that pig oocytes can be a useful model to assess human sperm functionality.

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“…These results are consistent with the concept that no selection pressure for species-specific binding exists in the murine reproductive system. In contrast to the avid binding to heterologous eggs shown by the epididymal sperm of mice and some other mammals, human sperm do not bind to foreign eggs except those of some other hominoids like the gibbon (37) and the lowland gorilla (58). The selection pressure that created this taxon-specific binding of human sperm is currently unknown.…”

Section: Why Continue To Employ Carbohydrate Recognition For Murine Gmentioning

confidence: 94%

Molecular Models for Murine Sperm-Egg Binding

Clark

Dell

2006

Journal of Biological Chemistry

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Murine sperm initiate fertilization by binding to the specialized extracellular matrix of mouse eggs, known as the zona pellucida. Over the past decade, powerful genetic, biophysical, and biochemical techniques have been employed to gain new insights into this interaction. Evidence from these studies does not support either of two major models for binding first proposed over two decades ago. Two more recently established models suggest that protein-protein interactions predominate during this initial stage of fertilization. Another model proposes that about 75-80% of the murine sperm bound to zona pellucida under well defined in vitro conditions is carbohydrate dependent, with the remaining sperm bound via protein-protein interactions. Mounting evidence suggests that the carbohydrate sequences coating the murine egg could be employed as specific immune recognition markers. Continued investigation of this system may resolve many of these controversial findings and reveal novel functions for murine zona pellucida glycoproteins.The species-specific binding of sperm to eggs is the initial event in the development of metazoans that propagate solely via sexual reproduction. Considerable evidence indicates that carbohydrate recognition plays a key role in this interaction in lower species (reviewed in Refs. 1-3), eutherian mammals (4, 5), and marsupials (6).The major animal model for investigating the role of carbohydrate recognition in mammalian fertilization is the mouse. This species is preferred because of its fecundity, short life span, low maintenance costs, and its ability to be genetically manipulated. Murine sperm initiate fertilization by binding to the mZP, 3 a matrix composed of three major glycoproteins designated mZP1, mZP2, and mZP3 (7). mZP3 has been implicated as the component that mediates both initial binding and the induction of the acrosome reaction (8). Its genetic deletion leads to the complete loss of a functional mZP and infertility (9). Therefore mZP3 is usually the primary glycoprotein targeted in functional studies. The Emergence of Major Models for Murine Sperm-Egg BindingTwo major hypothetical models for murine gamete binding were first presented in 1985. The resistance of mZP3 to denaturing conditions suggested that its protein-linked glycans could be responsible for initial sperm-egg binding (10). Subsequent studies demonstrated that either glycopeptides or O-linked glycans derived from mZP3 inhibit murine sperm-egg binding in a competitive murine sperm-egg binding assay (10, 11). Therefore Wassarman and colleagues suggested that EBPs on the sperm plasma membrane interact with mZP3 associated O-glycans to mediate initial murine sperm-egg binding.Digestion of the O-glycans derived from mZP3 with ␣-galactosidase results in the loss of their inhibitory activity in the murine sperm-egg binding assay, suggesting that terminal Gal␣1-3Gal sequence are crucial for binding (12). However, a later study confirmed that both terminal ␤l-4-linked Gal and its ␣1-3-galactosylated analogue (Gal␣1-3Gal␤1-...

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Hemizona assay for measuring zona binding in the lowland gorilla

Cited by 22 publications

References 15 publications

The specificity of human spermatozoa/zona pellucida interaction under hemizona assay conditions

The specificity of human spermatozoa/zona pellucida interaction under hemizona assay conditions

First Steps in the Development of a Functional Assay for Human Sperm Using Pig Oocytes

Molecular Models for Murine Sperm-Egg Binding

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