ArticlePloS one2013
Structural analysis of peptide-analogues of human Zona Pellucida ZP1 protein with amyloidogenic properties: insights into mammalian Zona Pellucida formation.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 37 citations in OpenAlex.
- A functional amyloid scaffold shapes insect egg coats.bioRxiv : the preprint server for biology · 2026Article
- Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023Review
- Amyloids and prions in the light of evolution.Current genetics · 2023Review
- Zona Pellucida Genes and Proteins: Essential Players in Mammalian Oogenesis and Fertility.Genes · 2021Review
- Human Zona Pellucida Glycoproteins: Binding Characteristics With Human Spermatozoa and Induction of Acrosome Reaction.Frontiers in cell and developmental biology · 2021Review
- A C. elegans Zona Pellucida domain protein functions via its ZPc domain.PLoS genetics · 2020Article
- Functional amyloids of eukaryotes: criteria, classification, and biological significance.Current genetics · 2020Review
- Zona pellucida genes and proteins and human fertility.Trends in developmental biology · 2020Article
- The epididymal amyloid matrix: structure and putative functions.Andrology · 2019Review
- RFAmyloid: A Web Server for Predicting Amyloid Proteins.International journal of molecular sciences · 2018Article
- AmyPro: a database of proteins with validated amyloidogenic regions.Nucleic acids research · 2018Article
- Functional Amyloids in Reproduction.Biomolecules · 2017Review
- Amyloid properties of the mouse egg zona pellucida.PloS one · 2015Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Zona pellucida (ZP) is an extracellular matrix surrounding and protecting mammalian and fish oocytes, which is responsible for sperm binding. Mammalian ZP consists of three to four glycoproteins, called ZP1, ZP2, ZP3, ZP4. These proteins polymerize into long interconnected filaments, through a common structural unit, known as the ZP domain, which consists of two domains, ZP-N and ZP-C. ZP is related in function to silkmoth chorion and in an evolutionary fashion to the teleostean fish chorion, also fibrous structures protecting the oocyte and embryo, that both have been proven to be functional amyloids. Two peptides were predicted as 'aggregation-prone' by our prediction tool, AMYLPRED, from the sequence of the human ZP1-N domain. Here, we present results from transmission electron microscopy, X-ray diffraction, Congo red staining and attenuated total reflectance Fourier-transform infrared spectroscopy (ATR FT-IR), of two synthetic peptide-analogues of these predicted 'aggregation-prone' parts of the human ZP1-N domain, that we consider crucial for ZP protein polymerization, showing that they both self-assemble into amyloid-like fibrils. Based on our experimental data, we propose that human ZP (hZP) might be considered as a novel, putative, natural protective amyloid, in close analogy to silkmoth and teleostean fish chorions. Experiments are in progress to verify this proposal. We also attempt to provide insights into ZP formation, proposing a possible model for hZP1-N domain polymerization.
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