Allorecognition mechanisms during ascidian fertilization

Int J Dev Biol. 2008;52(5-6):637-45. doi: 10.1387/ijdb.072544yh.

Abstract

Ascidians (primitive chordates) are hermaphroditic animals, releasing sperm and eggs nearly simultaneously. But, many ascidians, including Ciona intestinalis and Halocynthia roretzi, show self-sterility or preference for cross-fertilization rather than self-fertilization. The molecular mechanisms underlying this allorecognition process are only poorly understood. We recently identified the genes responsible for self-incompatibility in C. intestinalis by a positional cloning: sperm-borne polycystin 1-like receptor, referred to as s-Themis, and its fibrinogen-like ligand called v-Themis on the vitelline coat (VC) are highly polymorphic and appear to be responsible for allorecognition in the fertilization of C. intestinalis. In H. roretzi, on the other hand, we revealed that HrVC70, a 70-kDa main component of the VC consisting of 12 epidermal-growth-factor (EGF)-like repeats, is a candidate allorecognition protein, since the attachment of this protein to the VC during oocyte maturation and its detachment by weak acid are closely linked to the gain and the loss of self-sterility, respectively, and also since nonself-sperm rather than self-sperm efficiently bound to HrVC70-agarose. As a binding partner of HrVC70, a 35-kDa GPI-anchored glycoprotein in sperm lipid rafts, referred to as HrUrabin, was identified: HrUrabin appears to play a key role in allorecognizable sperm binding to HrVC70 during fertilization. In the present review, we describe the current progress on the molecular bases of allorecognition, or self-incompatibility, during ascidian fertilization, by considering the SI systems in another organisms including fungies and flowering plants.

Publication types

  • Review

MeSH terms

  • Animals
  • Ciona intestinalis
  • Cloning, Molecular
  • Epidermal Growth Factor / chemistry
  • Female
  • Fertilization*
  • Haploidy
  • Male
  • Models, Biological
  • Models, Genetic
  • Protein Binding
  • Sperm-Ovum Interactions
  • Urochordata / physiology*
  • Vitelline Membrane / chemistry
  • Vitelline Membrane / metabolism*

Substances

  • Epidermal Growth Factor