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Home / Equine Research Bank / Biol Reprod / Zonadhesin D3-polypeptides vary among species but are simila...
Biology of reproduction2009; 82(2); 413-421; doi: 10.1095/biolreprod.109.077891

Zonadhesin D3-polypeptides vary among species but are similar in Equus species capable of interbreeding.

Abstract: Zonadhesin is a rapidly evolving protein in the sperm acrosome that confers species specificity to sperm-zona pellucida adhesion. Though structural variation in zonadhesin likely contributes to its species-specific function, the protein has not previously been characterized in organisms capable of interbreeding. Here we compared properties of zonadhesin in several animals, including the horse (Equus caballus), donkey (E. asinus), and Grevy's zebra (E. grevyi) to determine if variation in zonadhesin correlates with ability of gametes to cross-fertilize. Zonadhesin localized to the apical acrosomes of spermatozoa from all three Equus species, similar to its localization in other animals. Likewise, in horse and donkey testis, zonadhesin was detected only in germ cells, first in the acrosomal granule of round spermatids and then in the developing acrosomes of elongating spermatids. Among non-Equus species, D3-domain polypeptides of mature, processed zonadhesin varied markedly in size and detergent solubility. However, zonadhesin D3-domain polypeptides in horse, donkey, and zebra spermatozoa exhibited identical electrophoretic mobility and detergent solubility. Equus zonadhesin D3-polypeptides (p110/p80 doublet) were most similar in size to porcine and bovine zonadhesin D3-polypeptides (p105). Sequence comparisons revealed that the horse zonadhesin precursor's domain content and arrangement are similar to those of zonadhesin from other large animals. Partial sequences of horse and donkey zonadhesin were much more similar to each other (>99% identity) than they were to orthologous sequences of human, pig, rabbit, and mouse zonadhesin (52%-72% identity). We conclude that conservation of zonadhesin D3-polypeptide properties correlates with ability of Equus species to interbreed.
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Publication Date: 2009-09-30 PubMed ID: 19794156PubMed Central: PMC2809229DOI: 10.1095/biolreprod.109.077891Google Scholar: Lookup
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  • Comparative Study
  • Journal Article
  • Research Support
  • N.I.H.
  • Extramural
  • Research Support
  • Non-U.S. Gov't

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The study examines zonadhesin, a protein in sperm that aids species-specific bonding to the egg’s protective layer, in different species. The study found that this protein’s properties in horse, donkey, and zebra are identical and likely contributing to their ability to interbreed, unlike other species with more significant differences.

Understanding Zonadhesin Protein

  • Zonadhesin is a protein that resides in the sperm’s acrosome, the part of a sperm cell that contains enzymes helping the sperm to penetrate the ovum.
  • This protein has been observed to evolve rapidly and contributes to species-specific adhesion between sperm and the egg’s surrounding layer known as the zona pellucida.

The Role of Zonadhesin in Interbreeding

  • The study aimed to investigate variations in zonadhesin in animals capable of interbreeding, which had not been explored before.
  • Analysis centered around zonadhesin in various animals, prominently the horse, donkey, and Grevy’s zebra, all part of the Equus genus and able to interbreed.
  • The researchers sought to uncover whether variations in this protein correlate with the capacity for cross-fertilization among these species.

Observations and Findings

  • Zonadhesin was found to be located in the apical acrosomes of spermatozoa in all three examined Equus species, similar to the positioning in other animals.
  • In both horses and donkey testes, zonadhesin existed only in germ cells, initially in the acrosomal granule of round spermatids and then in the developing acrosomes of elongating spermatids.
  • Non-Equus species presented greater variance in the size and detergent solubility of the zonadhesin D3-domain polypeptides, a part of the mature, processed zonadhesin protein.
  • Coinciding with the possibility of cross-fertilization, the zonadhesin D3-domain polypeptides in horse, donkey, and zebra spermatozoa showed identical properties when it came to electrophoretic mobility and detergent solubility.

Implications of Findings

  • The findings imply that the preservation of zonadhesin D3-polypeptide properties correlates with interbreeding capability in Equus species.
  • This could potentially pave the way for new research and understanding of reproductive biology and the mechanisms underpinning speciation and interbreeding among animals.

Cite This Article

APA
Tardif S, Brady HA, Breazeale KR, Bi M, Thompson LD, Bruemmer JE, Bailey LB, Hardy DM. (2009). Zonadhesin D3-polypeptides vary among species but are similar in Equus species capable of interbreeding. Biol Reprod, 82(2), 413-421. https://doi.org/10.1095/biolreprod.109.077891

Publication

Biology of reproduction
ISSN: 1529-7268
NlmUniqueID: 0207224
Country: United States
Language: English
Volume: 82
Issue: 2
Pages: 413-421

Researcher Affiliations

Tardif, Steve
  • Department of Cell Biology & Biochemistry, Texas Tech University Health Sciences Center, Lubbock, Texas 79430, USA.
Brady, Heidi A
    Breazeale, Kelly R
      Bi, Ming
        Thompson, Leslie D
          Bruemmer, Jason E
            Bailey, Laura B
              Hardy, Daniel M

                MeSH Terms

                • Acrosome / chemistry
                • Amino Acid Sequence
                • Animals
                • Breeding
                • Equidae / physiology
                • Female
                • Fertilization / physiology
                • Horses / physiology
                • Humans
                • Male
                • Membrane Proteins / analysis
                • Membrane Proteins / chemistry
                • Membrane Proteins / genetics
                • Molecular Sequence Data
                • Solubility
                • Species Specificity
                • Spermatozoa / chemistry
                • Spermatozoa / ultrastructure

                Grant Funding

                • HD-35166 / NICHD NIH HHS

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                Citations

                This article has been cited 8 times.
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