Spermatozoa from a marsupial, the brushtail possum, contain β1,4-galactosyltransferase

A. G. Braundmeier, William G. Breed, D. J. Miller

Research output: Contribution to journalArticlepeer-review


β1,4-Galactosyltransferase-I (GalTase-I) is one of the key molecules on the sperm surface of eutherian mammals that is likely to be involved in binding to the egg coat, the zona pellucida, to mediate sperm-egg interaction. In laboratory mice, the species for which most data are available, this protein functions as a receptor for the zona pellucida protein ZP3 of the oocyte and, upon binding, triggers the sperm acrosome reaction. In the present study, we investigated the presence and abundance of GalTase-I in epididymal sperm extracts of a marsupial, the brushtail possum, Trichosurus vulpecula. For this, spermatozoa were collected from cauda epididymides and the amount of β1,4-galactosyltransferase activity in washed sperm extracts was compared with that of porcine spermatozoa. Overall β1,4-galactosyltransferase enzyme activity was found to be more abundant in possum sperm extracts than those from porcine spermatozoa (P < 0.05). Immunoblots with an antibody to mouse GalTase-I revealed that the molecular weight of possum spermatozoa GalTase-I was 66 kDa, which is similar to the molecular weight of GalTase-I in spermatozoa from eutherian mammals. The molecular weight of GalTase-I was the same in sperm extracts collected from the caput and cauda epididymides. These results demonstrate that GalTase-I is indeed present in possum spermatozoa and thus it may be a gamete receptor molecule on the sperm surface of marsupials as well as those of eutherian mammals.

Original languageEnglish (US)
Pages (from-to)402-407
Number of pages6
JournalReproduction, Fertility and Development
Issue number3
StatePublished - 2008

ASJC Scopus subject areas

  • Genetics
  • Endocrinology
  • Animal Science and Zoology
  • Molecular Biology
  • Biotechnology
  • Reproductive Medicine
  • Developmental Biology


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