Recombinant prespore-specific antigen from Dictyostelium discoideum is a β-sheet glycoprotein with a spacer peptide modified by O-linked N-acetylglucosamine

Natasha E. Zachara, Nicolle H. Packer, Mark D. Temple, Martin B. Slade, Daniel R. Jardine, Peter Karuso, Catherine J. Moss, Bridget C. Mabbutt, Paul M. G. Curmi, Keith L. Williams*, Andrew A. Gooley

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

27 Citations (Scopus)


Prespore-specific antigen (PsA) is a putative cell-adhesion molecule of the cellular slime mould Dictyostelium discoideum, which has a similar molecular architecture to several mammalian cell-surface proteins. It has an N-terminal globular domain presented to the extracellular environment on an O-glycosylated stem (glycopeptide) that is attached to the cell membrane through a glycosyl-PtdIns anchor. The sequence of PsA suggests that PsA may belong to a new family of cell-surface molecules and here we present information on the structure of the N-terminal globular domain and determine the reducing-terminal linkage of the O-glycosylation. To obtain a sufficient amount of pure protein, a secreted recombinant form of PsA (rPsA), was expressed in D. discoideum and characterised. 1H-NMR spectra of rPsA contained features consistent with a high degree of β-sheet in the N-terminal globular domain, a feature commonly observed in cell-adhesion proteins. Solid-phase Edman degradation of the glycopeptide of rPsA indicated that 14 of the 15 threonines and serines in the spacer region were glycosylated. The chemical structures of the O-glycosylations were determined to be single N-acetylglucosamine residues.

Original languageEnglish
Pages (from-to)511-518
Number of pages8
JournalEuropean Journal of Biochemistry
Issue number2
Publication statusPublished - 1996


  • cell-surface glycoproteins
  • dictyostelium discoideum
  • N-acetylglucosamine
  • O-glycosylation


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