Evidence map›Paper›PMID 38490181›Full record

ArticleCell2024

ZP2 cleavage blocks polyspermy by modulating the architecture of the egg coat.

Shunsuke Nishio, Chihiro Emori, Benjamin Wiseman, Dirk Fahrenkamp, Elisa Dioguardi, Sara Zamora-Caballero, Marcel Bokhove, Ling Han, Alena Stsiapanava, Blanca Algarra and 10 more

Open access · hybridAbstract read
In one paragraph

Article in Cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
22.6field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

28 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Sperm, egg, and embryo proteins critical for genetic adaptation of herring to low salinity in the Baltic Sea.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. PES-8 is required for Cytoskeletal Organization and Contractility in thebioRxiv : the preprint server for biology · 2026
    Article
  8. Article
  9. Article
  10. Review
  11. Membrane Fusions During Mammalian Fertilization.Advances in experimental medicine and biology · 2026
    Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

20 authors at 6 institutions in 4 countries.

Shunsuke NishioDepartment of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden.
Chihiro EmoriDepartment of Experimental Genome Research, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, Japan; Immunology Frontier Research Center, Osaka University, Suita, Osaka, Japan.
Benjamin WisemanDepartment of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden.
Dirk FahrenkampDepartment of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden.
Elisa DioguardiDepartment of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden.
Sara Zamora-CaballeroDepartment of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden.
Marcel BokhoveDepartment of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden.
Ling HanDepartment of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden.
Alena StsiapanavaDepartment of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden.
Blanca AlgarraDepartment of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden.
Yonggang LuDepartment of Experimental Genome Research, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, Japan; Immunology Frontier Research Center, Osaka University, Suita, Osaka, Japan.
Mayo KodaniDepartment of Experimental Genome Research, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, Japan; Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Osaka, Japan.
Rachel E BainbridgeDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, PA, USA.
Kayla M KomondorDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, PA, USA.
Anne E CarlsonDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, PA, USA.
Michael LandrehDepartment of Microbiology, Tumor and Cell Biology, Karolinska Institutet, Stockholm, Sweden; Department of Cell and Molecular Biology, Uppsala University, 75124 Uppsala, Sweden.
Daniele de SanctisESRF - The European Synchrotron, Grenoble, France.
Shigeki YasumasuDepartment of Materials and Life Sciences, Faculty of Science and Technology, Sophia University, Tokyo, Japan.
Masahito IkawaDepartment of Experimental Genome Research, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, Japan; Immunology Frontier Research Center, Osaka University, Suita, Osaka, Japan; Graduate School of Pharmaceutical Sciences, Osaka University, Suita, Osaka, Japan; Center for Infectious Disease Education and Research (CiDER), Osaka University, Suita, Osaka, Japan.
Luca JovineDepartment of Biosciences and Nutrition, Karolinska Institutet, Huddinge, Sweden. Electronic address: luca.jovine@ki.se.
Karolinska Institutet · SEThe University of Osaka · JPUniversity of Pittsburgh · USEuropean Synchrotron Radiation Facility · FRSophia University · JPUppsala University · SE

Funding

Signaling Mechanisms of TMEM16a RegulationR01GM125638 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI CARLSON, ANNE E · 2018 to 2022
$1.6M
NIGMS NIH HHS R01 GM125638
6 · The paper itself

Abstract

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.

Indexed as

Zona Pellucida GlycoproteinsFemaleHumansMaleOvumSemenSpermatozoaZona PellucidaZona Pellucida GlycoproteinsZP2 protein, humanblock to polyspermyegg coat hardeningegg-sperm interactionfertilizationintegrative structural biologyzona pellucidaZP1ZP2 cleavageZP3ZP protein filament

Identifiers

PMID38490181
PMCPMC10976854
OpenAlexW4392801959

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.