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TitleZP2 cleavage blocks polyspermy by modulating the architecture of the egg coat.
Journal, issue, pagesCell, Vol. 187, Issue 6, Page 1440-1459.e24, Year 2024
Publish dateMar 14, 2024
AuthorsShunsuke Nishio / Chihiro Emori / Benjamin Wiseman / Dirk Fahrenkamp / Elisa Dioguardi / Sara Zamora-Caballero / Marcel Bokhove / Ling Han / Alena Stsiapanava / Blanca Algarra / Yonggang Lu / Mayo Kodani / Rachel E Bainbridge / Kayla M Komondor / Anne E Carlson / Michael Landreh / Daniele de Sanctis / Shigeki Yasumasu / Masahito Ikawa / Luca Jovine /
PubMed AbstractFollowing the fertilization of an egg by a single sperm, the egg coat or zona pellucida (ZP) hardens and polyspermy is irreversibly blocked. These events are associated with the cleavage of the N- ...Following the fertilization of an egg by a single sperm, the egg coat or zona pellucida (ZP) hardens and polyspermy is irreversibly blocked. These events are associated with the cleavage of the N-terminal region (NTR) of glycoprotein ZP2, a major subunit of ZP filaments. ZP2 processing is thought to inactivate sperm binding to the ZP, but its molecular consequences and connection with ZP hardening are unknown. Biochemical and structural studies show that cleavage of ZP2 triggers its oligomerization. Moreover, the structure of a native vertebrate egg coat filament, combined with AlphaFold predictions of human ZP polymers, reveals that two protofilaments consisting of type I (ZP3) and type II (ZP1/ZP2/ZP4) components interlock into a left-handed double helix from which the NTRs of type II subunits protrude. Together, these data suggest that oligomerization of cleaved ZP2 NTRs extensively cross-links ZP filaments, rigidifying the egg coat and making it physically impenetrable to sperm.
External linksCell / PubMed:38490181 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.9 - 4.6 Å
Structure data

EMDB-19276: Cryo-EM of tetrameric collagenase-cleaved Xenopus ZP2-N2N3 (cleaved xZP2-N2N3) (C1)
Method: EM (single particle) / Resolution: 4.6 Å

EMDB-19277: Cryo-EM of tetrameric collagenase-cleaved Xenopus ZP2-N2N3 (cleaved xZP2-N2N3) (C2)
Method: EM (single particle) / Resolution: 4.4 Å

PDB-8bqu:
Molecular basis of ZP3/ZP1 heteropolymerization: crystal structure of a native vertebrate egg coat filament
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-8rke:
Crystal structure of the complete N-terminal region of human ZP2 (hZP2-N1N2N3)
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

PDB-8rkf:
Crystal structure of the ZP-N1 and ZP-N2 domains of human ZP2 (hZP2-N1N2)
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

PDB-8rkg:
Crystal structure of tetrameric collagenase-cleaved Xenopus ZP2-N2N3 (cleaved xZP2-N2N3)
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-8rkh:
Crystal structure of the ZP-N2 and ZP-N3 domains of mouse ZP2 (mZP2-N2N3)
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-8rki:
Molecular basis of ZP3/ZP1 heteropolymerization: crystal structure of a native vertebrate egg coat filament fragment
Method: X-RAY DIFFRACTION / Resolution: 4.2 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-HOH:
WATER / Water

ChemComp-NO3:
NITRATE ION / Nitrate

ChemComp-BCN:
BICINE / pH buffer*YM / Bicine

ChemComp-YB:
YTTERBIUM (III) ION / Ytterbium

Source
  • xenopus laevis (African clawed frog)
  • oryzias latipes (Japanese medaka)
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsSTRUCTURAL PROTEIN / Cell adhesion / fertilization / egg-sperm interaction / gamete recognition / sperm receptor / extracellular matrix / egg coat / zona pellucida / vitelline envelope / fish chorion / glycoprotein / N-glycan / ZP module / ZP-N domain / ZP_C domain / trefoil domain / medaka / Japanese rice fish / block to polyspermy / post-fertilization cleavage / ovastacin / AlphaFold / ZP-C domain

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