TY - JOUR
T1 - Schistosoma mansoni
T2 - Characterization of an α1-3 fucosyltransferase in adult parasites
AU - DeBose-Boyd, Russell
AU - Nyame, A. Kwame
AU - Cummings, Richard D.
N1 - Funding Information:
This work was supported by NIH Grant AI26725 to R.D.C. We thank Ms. Liying Yan for providing the TPA-EMphaze columns, Mr. Juinn-Chern Yeh for helpful assistance with Dionex analyses, Dr. Ki-Young Do for critical reading of the manuscript, and Dr. Qun Zhou for helpful advice in performing assays.
PY - 1996/1
Y1 - 1996/1
N2 - 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.
AB - 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.
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U2 - 10.1006/expr.1996.0001
DO - 10.1006/expr.1996.0001
M3 - Article
C2 - 8617325
AN - SCOPUS:0344004701
SN - 0014-4894
VL - 82
SP - 1
EP - 10
JO - Experimental Parasitology
JF - Experimental Parasitology
IS - 1
ER -