Glycan chains play a role in the axonemal cytoskeleton disassembly activity of the 35 kDa glycoprotein of the spermathecal extract of Eyprepocnemis plorans (Insecta, Orthoptera)

Andrea Giuffrida, Riccardo Focarelli, Raffaella Lampariello, Floriana Rosati

Research output: Contribution to journalArticlepeer-review

1 Scopus citations

Abstract

In a previous study we found that a glycoprotein (gp35), purified from spermathecal extract of the orthopteran Eyprepocnemis plorans, induced a disassembly process of the flagellum similar to that observed in some of the sperm stored in the spermatheca in 95% of the sperm tested (Giuffrida et al., 1996). In the present study the glycan chains of the protein were analysed by means of lectins and carbohydrate composition by high performance anionexchange chromatography. The gp35 was found to bear O- and N-linked glycans. The presence of mannose in the monosaccharide composition, as well as the negativity of the protein to ConA, suggested that the N-linked chains were of the complex trior tetra antennary type. The protein was positive to RCA, DSA and LTA thus suggesting the presence of terminal residues of galactose and fucose. The role of the glycan chains in the protein activity was investigated by deglycosylating gp35 with trifluoromethanesulfonic acid (TFMSA) and using different carbohydrates in competition assays. The results showed that the deglycosylated protein is inactive and that galactose is the only sugar able to reduce the native protein activity to approximately 50%.

Original languageEnglish (US)
Pages (from-to)315-321
Number of pages7
JournalInsect Biochemistry and Molecular Biology
Volume27
Issue number4
DOIs
StatePublished - Apr 1 1997
Externally publishedYes

Keywords

  • Axonemes
  • Glycoproteins
  • Insects
  • Lectins
  • Oligosaccharides
  • Sperm
  • Spermatheca

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Insect Science

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