Identification and characterization of a 38 kDa glycoprotein functionally associated with mating activity of Paramecium primaurelia

Marzia Ognibene, Cinzia Della Giovampaola, Francesca Trielli, Riccardo Focarelli, Floriana Rosati, Maria Umberta Delmonte Corrado

Research output: Contribution to journalArticlepeer-review

Abstract

In Paramecium primaurelia mating interactions take place immediately after mixing mating-competent cells of opposite mating types. The cells clump in clusters (mating reaction) and then separate in pairs. Previous results have shown that sialic acid-containing glycoconjugates are present on the cell surface and are involved in mating-cell pairing. In order to identify the sialic acid-containing glycoprotein(s), we first metabolically radiolabelled non-mating-competent cells with d-[6-3H]galactose, and then analyzed the radiolabelled proteins by anion exchange chromatography. We characterized a 38 kDa (gp38) sialic acid-containing glycoprotein and raised the corresponding polyclonal antibody by means of which we localized the antigen at the level of the oral region of non-mating-competent cells and on the ciliary surface of mating-competent cells. Immunoblot analysis of the ciliary protein fraction showed that the anti-gp38 serum interacted with a 38 kDa protein in both mating types I and II cells. We also demonstrated the functional activity of gp38 in the mating reaction by means of anti-gp38 antibody competition assays.

Original languageEnglish
Pages (from-to)81-90
Number of pages10
JournalEuropean Journal of Protistology
Volume44
Issue number2
DOIs
Publication statusPublished - May 30 2008

Keywords

  • Ciliates
  • Glycoproteins
  • Mating cell-cell interactions
  • Paramecium
  • Signal molecules

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)
  • Agricultural and Biological Sciences (miscellaneous)
  • Microbiology

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