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During fertilization, a sperm must first fuse with the plasma membrane and then penetrate the female egg cell to fertilize it. Fusing to the egg cell usually causes little problem, whereas penetrating through the egg's hard shell or extracellular matrix can be more difficult. Therefore, sperm cells go through a process known as the acrosome reaction, which is the reaction that occurs in the acrosome of the sperm as it approaches the egg.
The zona pellucida is a specialized extracellular matrix that surrounds the plasma membrane of mammalian oocytes. It is a vital constitutive part of the oocyte. The zona pellucida first appears in unilaminar primary oocytes. It is secreted by both the oocyte and the ovarian follicles. The zona pellucida is surrounded by the corona radiata. The corona is composed of cells that care for the egg when it is emitted from the ovary.
Acrosin is a digestive enzyme that acts as a protease. In humans, acrosin is encoded by the ACR gene. Acrosin is released from the acrosome of spermatozoa as a consequence of the acrosome reaction. It aids in the penetration of the Zona Pellucida.
Human fertilization is the union of an egg and sperm, occurring primarily in the ampulla of the fallopian tube. The result of this union leads to the production of a fertilized egg called a zygote, initiating embryonic development. Scientists discovered the dynamics of human fertilization in the 19th century.
The vitelline membrane or vitelline envelope is a structure surrounding the outer surface of the plasma membrane of an ovum or, in some animals, the extracellular yolk and the oolemma. It is composed mostly of protein fibers, with protein receptors needed for sperm binding which, in turn, are bound to sperm plasma membrane receptors. The species-specificity between these receptors contributes to prevention of breeding between different species. It is called zona pellucida in mammals. Between the vitelline membrane and zona pellucida is a fluid-filled perivitelline space.
Mothers against decapentaplegic homolog 3 also known as SMAD family member 3 or SMAD3 is a protein that in humans is encoded by the SMAD3 gene.
Uromodulin (UMOD), also known as Tamm–Horsfall protein (THP), is a zona pellucida-like domain-containing glycoprotein that in humans is encoded by the UMOD gene. Uromodulin is the most abundant protein excreted in ordinary urine.
Endoglin (ENG) is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex. It is also commonly referred to as CD105, END, FLJ41744, HHT1, ORW and ORW1. It has a crucial role in angiogenesis, therefore, making it an important protein for tumor growth, survival and metastasis of cancer cells to other locations in the body.
Sialyl LewisX (sLeX), also known as cluster of differentiation 15s (CD15s) or stage-specific embryonic antigen 1 (SSEA-1), is a tetrasaccharide carbohydrate which is usually attached to O-glycans on the surface of cells. It is known to play a vital role in cell-to-cell recognition processes. It is also the means by which an egg attracts sperm; first, to stick to it, then bond with it and eventually form a zygote.
Transforming growth factor alpha (TGF-α) is a protein that in humans is encoded by the TGFA gene. As a member of the epidermal growth factor (EGF) family, TGF-α is a mitogenic polypeptide. The protein becomes activated when binding to receptors capable of protein kinase activity for cellular signaling.
Zona pellucida sperm-binding protein 3, also known as zona pellucida glycoprotein 3 (Zp-3) or the sperm receptor, is a ZP module-containing protein that in humans is encoded by the ZP3 gene. ZP3 is the glycoprotein in the zona pellucida most important for inducting the acrosome reaction of sperm cells at the beginning of fertilization.
Zona pellucida sperm-binding protein 2 is a protein that in humans is encoded by the ZP2 gene.
Zona pellucida sperm-binding protein 4, ZP-4 or avilesine, named after its discoverer Manuel Avilés Sánchez is a protein that in humans is encoded by the ZP4 gene.
The alae is a protruding ridge that forms longitudinally on many nematodes. In the Caenorhabditis elegans nematode they are present in the L1, dauer and adult stages. The alae are most pronounced during the dauer larval stage and not present in the L2, and L3 C. elegans stages.
Folliculogenesis-specific basic helix-loop-helix, also known as factor in the germline alpha (FIGalpha) or transcription factor FIGa, is a protein that in humans is encoded by the FIGLA gene. The FIGLA gene is a germ cell-specific transcription factor preferentially expressed in oocytes that can be found on human chromosome 2p13.3.
Zona pellucida sperm-binding protein 1 is a protein that cross-links ZP2 and ZP3. Aberrant ZP1 results in sequestration of ZP3 in the cytoplasm, thereby preventing the formation of the zona pellucida around the oocyte.
Juno also known as folate receptor 4, folate receptor delta or IZUMO1R is a protein that in humans is encoded by the FOLR4 gene. Juno is a member of the folate receptor family and is GPI-anchored to the plasmalemma of the mammalian egg cell that recognizes its sperm-riding counterpart, IZUMO1, and facilitates fertilization. The protein was named after Juno, the Roman goddess of fertility and marriage.
Beta-sandwich, β-sandwich domains consisting of 80 to 350 amino acids occur commonly in proteins. They are characterized by two opposing antiparallel beta sheets (β-sheets). The number of strands found in such domains may differ from one protein to another. β-sandwich domains are subdivided in a variety of different folds. The immunoglobulin-type fold found in antibodies (Ig-fold) consists of a sandwich arrangement of 7 and 9 antiparallel β-strands arranged in two β-sheets with a Greek-key topology. The Greek-key topology is also found in Human Transthyretin. The jelly-roll topology is found in carbohydrate binding proteins such as concanavalin A and various lectins, in the collagen binding domain of Staphylococcus aureus Adhesin and in modules that bind fibronectin as found in Tenascin. The L-type lectin domain is a variation of the jelly roll fold. The C2 domain in its typical version (PKC-C2) is a β-sandwich composed of 8 beta-strands (β-strands).
The transforming growth factor beta (TGFβ) receptors are a family of serine/threonine kinase receptors involved in TGF beta signaling pathway. These receptors bind growth factor and cytokine signaling proteins in the TGF-beta family such as TGFβs, bone morphogenetic proteins (BMPs), growth differentiation factors (GDFs), activin and inhibin, myostatin, anti-Müllerian hormone (AMH), and NODAL.
Paul Michael Wassarman is an American biologist who has been Professor in the Dept. of Cell, Developmental, and Regenerative Biology at the Icahn School of Medicine at Mount Sinai since 1996. His laboratory identified and characterised proteins that make up the zona pellucida (ZP) of mammalian eggs and determined their role in fertilisation.
References
- 1 2 Bork P, Sander C (1992). "A large domain common to sperm receptors (Zp2 and Zp3) and TGF-beta type III receptor". FEBS Lett. 300 (3): 237–40. doi: 10.1016/0014-5793(92)80853-9 . PMID 1313375. S2CID 38778076.
- 1 2 Jovine L, Darie CC, Litscher ES, Wassarman PM (2005). "Zona pellucida domain proteins". Annu. Rev. Biochem. 74: 83–114. doi:10.1146/annurev.biochem.74.082803.133039. PMID 15952882.
- ↑ Jovine L, Qi H, Williams Z, Litscher E, Wassarman PM (2002). "The ZP domain is a conserved module for polymerization of extracellular proteins". Nat. Cell Biol. 4 (6): 457–61. doi:10.1038/ncb802. PMID 12021773. S2CID 11575790.
- ↑ Jovine L, Qi H, Williams Z, Litscher ES, Wassarman PM (2004). "A duplicated motif controls assembly of zona pellucida domain proteins". Proc. Natl. Acad. Sci. U.S.A. 101 (16): 5922–7. Bibcode:2004PNAS..101.5922J. doi: 10.1073/pnas.0401600101 . PMC 395899 . PMID 15079052.
- 1 2 3 Monné M, Han L, Schwend T, Burendahl S, Jovine L (2008). "Crystal structure of the ZP-N domain of ZP3 reveals the core fold of animal egg coats". Nature. 456 (7222): 653–7. Bibcode:2008Natur.456..653M. doi:10.1038/nature07599. hdl: 11563/8930 . PMID 19052627. S2CID 4430083. PDB: 3D4C, 3D4G, 3EF7
- 1 2 Han L, Monné M, Okumura, H, Schwend, T, Cherry, AL, Flot, D, Matsuda, T, Jovine, L (2010). "Insights into egg coat assembly and egg-sperm interaction from the X-ray structure of full-length ZP3". Cell. 143 (3): 404–15. doi: 10.1016/j.cell.2010.09.041 . hdl: 11563/8931 . PMID 20970175. S2CID 18583237. PDB: 3NK3, 3NK4
- ↑ Lin SJ, Hu Y, Zhu J, Woodruff TK, Jardetzky TS (2011). "Structure of betaglycan zona pellucida (ZP)-C domain provides insights into ZP-mediated protein polymerization and TGF-beta binding". Proc Natl Acad Sci U S A. 108 (13): 5232–6. Bibcode:2011PNAS..108.5232L. doi: 10.1073/pnas.1010689108 . PMC 3069177 . PMID 21402931. PDB: 3QW9
- ↑ Diestel U, Resch M, Meinhardt K, Weiler S, Hellmann TV, Mueller TD, Nickel J, Eichler J, Muller YA (2013). "Identification of a Novel TGF-β-Binding Site in the Zona Pellucida C-terminal (ZP-C) Domain of TGF-β-Receptor-3 (TGFR-3)". PLOS ONE. 8 (6): e67214. Bibcode:2013PLoSO...867214D. doi: 10.1371/journal.pone.0067214 . PMC 3695229 . PMID 23826237. PDB: 4AJV
- 1 2 Bokhove M, Nishimura K, Brunati M, Han L, de Sanctis D, Rampoldi L, Jovine L (2016). "A structured interdomain linker directs self-polymerization of human uromodulin". Proc. Natl. Acad. Sci. U.S.A. 113 (6): 1552–1557. Bibcode:2016PNAS..113.1552B. doi: 10.1073/pnas.1519803113 . PMC 4760807 . PMID 26811476. PDB: 4WRN, 5BUP
- ↑ Bokhove M, Jovine L (2018). "Structure of Zona Pellucida Module Proteins". Curr. Top. Dev. Biol. Current Topics in Developmental Biology. 130: 413–442. doi:10.1016/bs.ctdb.2018.02.007. ISBN 9780128098028. PMID 29853186.
- ↑ Saito T, Bokhove M, Croci R, Zamora-Caballero S, Han L, Letarte M, de Sanctis D, Jovine L (2017). "Structural Basis of the Human Endoglin-BMP9 Interaction: Insights into BMP Signaling and HHT1". Cell Reports. 19 (9): 1917–1928. doi:10.1016/j.celrep.2017.05.011. PMC 5464963 . PMID 28564608. PDB: 5HZV
- ↑ Stsiapanava A, Xu C, Brunati M, Zamora-Caballero S, Schaeffer C, Bokhove M, Han L, Hebert H, Carroni M, Yasumasu S, Rampoldi L, Wu B, Jovine L (2020). "Cryo-EM structure of native human uromodulin, a zona pellucida module polymer". EMBO J. 39 (24): e106807. doi: 10.15252/embj.2020106807 . PMC 7737619 . PMID 33196145. bioRxiv 10.1101/2020.05.28.119206 PDB: 6TQK, 6TQL
- ↑ Stsiapanava A, Xu C, Nishio S, Han L, Yamakawa N, Carroni M, Tunyasuvunakool K, Jumper J, de Sanctis D, Wu B, Jovine L (2022). "Structure of the decoy module of human glycoprotein 2 and uromodulin and its interaction with bacterial adhesin FimH". Nat. Struct. Mol. Biol. 29 (3): 190–193. doi: 10.1038/s41594-022-00729-3 . PMC 8930769 . PMID 35273390. PDB: 7PFP, 7Q3N
- ↑ Callebaut I, Mornon JP, Monget P (2007). "Isolated ZP-N domains constitute the N-terminal extensions of Zona Pellucida proteins". Bioinformatics. 23 (15): 1871–1874. doi: 10.1093/bioinformatics/btm265 . PMID 17510169.
- ↑ Raj I, Sadat Al Hosseini H, Dioguardi E, Nishimura K, Han L, Villa A, de Sanctis D, Jovine L (2017). "Structural Basis of Egg Coat-Sperm Recognition at Fertilization". Cell. 169 (7): 1315–1326. doi:10.1016/j.cell.2017.05.033. PMC 5480393 . PMID 28622512. PDB: 5II4, 5II5, 5II6, 5MR2, 5IIC, 5IIA, 5IIB, 5MR3
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