Schistosoma mansoni: Characterization of an α1-3 fucosyltransferase in adult parasites

Russell DeBose-Boyd, A. Kwame Nyame, Richard D. Cummings

Research output: Contribution to journalArticle

30 Scopus citations

Abstract

We report that extracts of Schistosoma mansoni contain a GDPFuc:Galβ1-4GlcNac (Fuc to GlcNAc) α1-3 fucosyltransferase (α1,3FT) capable of synthesizing the antigenic determinant known as Lewis x (Le(x), Galβ1-4[Fucα1-3]GlcNAcβ1-R). When the acceptor lacto-N-neotetraose (LNnt, Galβ1-4GlcNAcβ1-3Galβ1-4Glc) was incubated with extracts of S. manosoni in the presence of GDPFuc and Mn2, Fuc was transferred to generate the pentasaccharide lacto-N-fucopentaose III (LNFPIII, Galβ1-4[Fucα1-3Galβ1-4Glc). The enzyme did not transfer efficiently to the isomeric oligosaccharide lacto-N-tetraose (LNT, Galβ1-3GlcNAcβ1-3Galβ1-4Glc. The activity of the schistosome α1,3FT toward LNnT was dependent upon time, protein, and GDPFuc. Interestingly, the schistosome α1,3FT was also able to transfer Fuc to a sialic acid-containing trisaccharide NeuAcα2-3Galβ1-4GlcNAc to produce the tetrasaccharide sialyl Lewis x (2,3 sLe(x), NeuAcα2-3Galβ1-4[Fuc1-3]GlcNAc, although the rate of reaction with the sialylated acceptor was <5% of the rate obtained toward nonsialylated acceptor. The schistosome α1,3FT was relatively resistant to inhibition by N-ethylmaleimide. The enzymatic properties of the schistosome α1,3FT resemble those of the human myeloid fucosyltransferase FTIV and not those of other known human focosyltransferases.

Original languageEnglish (US)
Pages (from-to)1-10
Number of pages10
JournalExperimental Parasitology
Volume82
Issue number1
DOIs
StatePublished - Jan 1996

ASJC Scopus subject areas

  • Parasitology
  • Immunology
  • Infectious Diseases

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