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The bioactivities of the central segment of Zp2 polypeptide

Published online by Cambridge University Press:  19 May 2016

Zuowu Cao ,
Chuncheng Nie ,
Yan Xie  and
Dongqin Cai
Zuowu Cao*
Affiliation:
Department of Developmental and Regenerative Biology, Jinan University, Guangzhou 510632, China. Department of Developmental and Regenerative Biology, Jinan University, Guangzhou 510632, China.
Chuncheng Nie
Affiliation:
Department of Developmental and Regenerative Biology, Jinan University, Guangzhou 510632, China.
Yan Xie
Affiliation:
Department of Developmental and Regenerative Biology, Jinan University, Guangzhou 510632, China.
Dongqin Cai
Affiliation:
Department of Developmental and Regenerative Biology, Jinan University, Guangzhou 510632, China. Key Laboratory for Regenerative Medicine, Ministry of Education, Jinan University, Guangzhou 510632, China.
*
All correspondence to: Zuowu Cao. Department of Developmental and Regenerative Biology, Jinan University, Guangzhou 510632, China. E-mail: caozuowu@ymail.com
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Summary

In order to understand the role of the protein zona pellucida 2 in fertilization, an antibody against a central segment of the zona pellucida 2 peptide, segment 190–505 (Z2eH), was prepared. The influence of the antibody on sperm–zona interaction was tested using the sperm–egg binding assay. The effect of the antibody on fertility was evaluated by passive immunization with anti-Z2eH antibody. Immunohistochemical assay showed that an antibody from rabbit reacted specifically with the natural zona pellucida on mouse ovarian sections. Immunofluorescence assay showed that the antibody bound specifically to the zonae pellucidae of the ovulated oocytes and 2-cell embryos after passive immunization. The antibody-treated oocytes bound capacitated sperm as control oocytes, passive immunization did not impede the action of sperm to fertilize the oocyte in vivo. These findings suggest that the central peptide of ZP2 (190–505) is immunogenic and contains zona pellucida-specific epitopes, however the central polypeptide might not be the crucial part from which to construct a functional domain to bind sperm.

Keywords

AntibodyImmunofluorescenceMouse zona pellucida 2 (ZP2)Passive immunizationSperm–egg binding
Type
Research Article
Information
Zygote , Volume 24 , Issue 5 , October 2016 , pp. 768 - 774
Copyright
Copyright © Cambridge University Press 2016 

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References

Baibakov, B., Gauthier, L., Talbot, P., Rankin, T.L. & Dean, J. (2007). Sperm binding to the zona pellucida is not sufficient to induce acrosome exocytosis. Development 134, 933–43.Google Scholar
Baibakov, B., Boggs, N.A., Yauger, B., Baibakov, G. & Dean, J. (2012). Human sperm bind to the N-terminal domain of ZP2 in humanized zonae pellucidae in transgenic mice. J. Cell Biol. 197, 897–905.Google Scholar
Beebe, S.J., Leyton, L., Burks, D., Ishikawa, M., Fuerst, T., Dean, J. & Saling, P. (1992). Recombinant mouse ZP3 inhibits sperm binding and induces the acrosome reaction. Dev. Biol. 151, 48–54.Google Scholar
Bleil, J.D. & Wassarman, P.M. (1986). Autoradiographic visualization of the mouse egg's sperm receptor bound to sperm. J. Cell Biol. 102, 1363–71.Google Scholar
Bleil, J.D., Greve, J.M. & Wassarman, P.M. (1988). Identification of a secondary sperm receptor in the mouse egg zona pellucida: role in maintenance of binding of acrosome-reacted sperm to eggs. Dev. Biol. 128, 376–85.Google Scholar
East, A.J., Mattison, D.R. & Dean, J. (1984). Monoclonal antibodies to the major protein of the murine zona pellucida: effects on fertilization and early development. Dev. Biol. 104, 49–56.Google Scholar
East, I.J. & Dean, J. (1984). Monoclonal antibodies as probes of the distribution of ZP-2, the major sulphated glycoprotein of the murine zona pellucida. J. Cell Biol. 9S, 795–800.Google Scholar
Gahlay, G., Gauthier, L., Baibakov, B., Epifano, O. & Dean, J. (2010). Gamete recognition in mice depends on the cleavage status of an egg's zona pellucida protein. Science 329, 216–9.Google Scholar
Hinsch, E., Hagele, W., Bohle, R.M., Schill, W.B. & Hinsch, K.D. (1998). Evaluation of ZP2 domains of functional importance against synthetic ZP2 peptides. J. Reprod. Fertil. 114, 245–51.Google Scholar
Kinloch, R.A., Mortillo, S. & Stewart, C.L. (1991). Embryonal carcinoma cells transfected with ZP3 genes differentially glycosylate similar polypeptides and secrete active mouse sperm receptor. J. Cell Biol. 115, 655–64.Google Scholar
Lea, I.A., Widgren, E.E. & O'Rand, M.G. (2002). Analysis of recombinant mouse zona pellucida protein 2 (ZP2) constructs for immunocontraception. Vaccine 22, 1515–23.CrossRefGoogle Scholar
Liang, L.F., Chamow, S.M. & Dean, J. (1990). Oocyte-specific expression of mouse Zp-2: developmental regulation of the zona pellucida genes. Mol. Cell. Biol. 10, 1507–15.Google Scholar
Mortillo, S. & Wassarman, P.M. (1991). Differential binding of gold-labelled zona pellucida glycoproteins Zp2 and mZP3 to mouse sperm membrane compartments. Development 113, 141–9.Google Scholar
Sun, W., Lou, Y., Dean, J. & Tung, K.S.K. (1999). A contraceptive peptide vaccine targeting sulphated glycoprotein ZP2 of the mouse zona pellucida. Biol. Reprod. 60, 900–7.CrossRefGoogle ScholarPubMed
Tsubamoto, H., Hasegawa, A., Nakata, Y., Naito, S., Yamasaki, N. & Koyama, K. (1999). Expression of recombinant human zona pellucida protein 2 and its binding capacity to spermatozoa. Biol. Reprod. 61, 1649–54.Google Scholar
van Duin, M., Polman, J.E., De Breet, I.T., van Ginneken, K., Bunschoten, H., Grootenhuis, A., Brindle, J. & Aitken, R.J. (1994). Recombinant human zona pellucida protein ZP3 produced by Chinese hamster ovary cells induces the human sperm acrosome reaction and promotes sperm–egg fusion. Biol. Reprod. 51, 607–17.Google Scholar
Wassarman, P.M. (1990). Profile of a mammalian sperm receptor. Development 108, 1–17.Google Scholar