Inhibition by anti‐sperm monoclonal antibodies of the penetration of zona‐free hamster oocytes by human spermatozoa

García-Framis, V.; Martorell, R.; Márquez, Carmen; Benet, J.; Andolz, P.; Martı́nez, Paz

doi:10.1038/icb.1994.1

Cited by 16 publications

(2 citation statements)

References 14 publications

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“…There are a number of antibodies like OBF13 (the antibody that identified Izumo, Section 3.1.1) that perturb sperm-egg binding and/or fusion, but the antigens of these antibodies remain unidentified or only partially characterized (116)(117)(118)(119)(120)(121)(122). One of potential interest is sperad, an IgSF member like Izumo (Section 3.1.1).…”

Section: Antigens Implicated In Sperm-egg Interactions By Fertilizatimentioning

confidence: 99%

New insights into the molecular basis of mammalian sperm-egg membrane interactions

Vjugina¹

2008

Front Biosci

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Fertilization is the process by which two terminally differentiated cells, the sperm and the egg, merge to form a totipotent cell, the zygote. This review addresses one of the culminating steps in getting sperm and egg together: the cell-cell interactions that allow the two gametes to fuse and create the zygote. Based on cell biological and genetic studies, major players include CD9 on the egg and Izumo on the sperm, although other molecules are part of an ever-evolving discussion of models for the molecular mechanisms leading to sperm-egg fusion, since few molecules have been shown to be completely essential for sperm-egg union. This sets the stage for consideration of how genetic approaches impact the field--of how knockout mouse reproductive phenotypes translate to humans and other animals and also of how interactions between redundant, nonessential genes could affect reproductive processes such as gamete interaction ("synthetic infertility," analogous to synthetic lethality). We will address these issues, examine the molecular basis of sperm-egg union and how this field has evolved with modern approaches combined with classical studies, and also discuss basic research in gamete biology in light of its possible application to reproductive health.

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Section: Antigens Implicated In Sperm-egg Interactions By Fertilizatimentioning

confidence: 99%

New insights into the molecular basis of mammalian sperm-egg membrane interactions

Vjugina¹

2008

Front Biosci

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“…Unfortunately, egg molecules can be extremely difficult to characterize due to a paucity of material (25 ng of protein per mouse egg, and 20-50 eggs can be retrieved per superovulated mouse). Other candidate molecules include the antigens of antibodies that inhibit sperm-egg binding or fusion (127)(128)(129)(130)(131).…”

Section: Other Moleculesmentioning

confidence: 99%

Sperm disintegrins egg integrins and other cell adhesion molecules of mammalian gamete plasma membrane interactions

Evans¹

1999

Front Biosci

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Introduction to Fertilization 3. Methods used to study sperm-egg interactions 3.1. Detecting sperm-egg fusion 3.2. Detecting sperm-egg binding 3.3. IVF assays: ZP-intact and ZP-free eggs, and homologous versus heterologous systems 4. Sperm disintegrins 4.1. General information on ADAM/MDC family members 4.2. Fertilin beta (ADAM2) 4.3. Fertilin alpha (ADAM1) 4.4. Cyritestin (ADAM3, tMDCI) 5. Egg integrins as receptors for sperm and sperm disintegrins 5.1. Integrins on mammalian eggs 5.2. Alpha-6/beta-1 integrins as receptors for sperm and for sperm disintegrins 6. Other molecules involved in sperm-egg interactions 6.1. DE/CRISP-1 6.2. Extracellular matrix proteins 6.3. Complement components 6.4. Other molecules 7. Summary, conclusions, and future directions 8. Acknowledgements 9. References

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Characterization of the Binding of Recombinant Mouse Sperm Fertilin β Subunit to Mouse Eggs: Evidence for Adhesive Activity via an Egg β1Integrin-Mediated Interaction

Evans

Kopf

Schultz

1997

Developmental Biology

145

127

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The sperm protein fertilin (also known as PH-30) is a candidate for mediating the interactions between sperm and egg plasma membranes. Fertilin is a heterodimer. The beta subunit, which has a region with homology to the family of integrin ligands known as disintegrins, has been hypothesized to be involved in the binding of sperm to the egg surface. To investigate this hypothesis and determine what role fertilin beta plays in fertilization, we have expressed the putative extracellular domain of mouse fertilin beta in bacteria as a fusion protein with maltose-binding protein (hereafter referred to as recombinant fertilin beta-EC) and used two assays to characterize its binding to mouse eggs. Immunocytochemistry was used to examine the localization of recombinant fertilin beta-EC binding. A luminometric assay was also developed to quantify levels of binding of recombinant fertilin beta-EC to single eggs. We find that recombinant fertilin beta-EC binds to the region of the plasma membrane of the egg to which sperm bind, thus providing the first direct evidence that fertilin beta has adhesive properties. Peptides corresponding to the disintegrin domain of fertilin beta reduce its binding to eggs, suggesting that this domain is at least partially involved in the recognition of fertilin beta by binding sites on the egg. Treatment of zona pellucida-free eggs with chymotrypsin reduces the ability of the eggs to support the binding of recombinant fertilin beta-EC, implicating an egg surface protein as a binding site for recombinant fertilin beta-EC. Binding of recombinant fertilin beta-EC to eggs is also reduced in the absence of divalent cations and is supported by 2.0 mM Ca2+, Mg2+, or Mn2+. Furthermore, eggs incubated in recombinant fertilin beta-EC prior to in vitro fertilization show reduced levels of sperm binding. Finally, we have examined the possible role of integrins on eggs as receptors for fertilin beta, since an anti-alpha6 integrin subunit monoclonal antibody, GoH3, has been shown to inhibit sperm binding (E. A. C. Almeida et al. (1995) Cell 81, 1095-1104). We find that: (a) an increased amount of GoH3 epitope on the egg surface does not correlate with an increased ability of the eggs to bind sperm or recombinant fertilin beta-EC; (b) the GoH3 antibody has virtually no inhibitory effect on recombinant fertilin beta-EC binding; and (c) recombinant fertilin beta-EC binding is reduced in the presence of anti-beta1 integrin antibodies. These results suggest that a beta1-containing integrin participates in the binding of recombinant fertilin beta-EC to mouse eggs.

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Inhibition by anti‐sperm monoclonal antibodies of the penetration of zona‐free hamster oocytes by human spermatozoa

Cited by 16 publications

References 14 publications

New insights into the molecular basis of mammalian sperm-egg membrane interactions

New insights into the molecular basis of mammalian sperm-egg membrane interactions

Sperm disintegrins egg integrins and other cell adhesion molecules of mammalian gamete plasma membrane interactions

Characterization of the Binding of Recombinant Mouse Sperm Fertilin β Subunit to Mouse Eggs: Evidence for Adhesive Activity via an Egg β1Integrin-Mediated Interaction

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