Abstract
Core β-1,2-xylose and α-1,3-fucose are antigenic motifs on schistosome N-glycans, as well as prominent IgE targets on some plant and insect glycoproteins. To map the association of schistosome infection with responses to these motifs, we assessed plasma IgE and IgG reactivity using microarray technology among Ugandans from rural Schistosoma mansoni (Sm)-endemic islands (n = 209), and from proximate urban communities with lower Sm exposure (n = 62). IgE and IgG responses to core β-1,2-xylose and α-1,3-fucose modified N-glycans were higher in rural versus urban participants. Among rural participants, IgE and IgG to core β-1,2-xylose were positively associated with Sm infection and concentration peaks coincided with the infection intensity peak in early adolescence. Responses to core α-1,3-fucose were elevated regardless of Sm infection status and peaked before the infection peak. Among urban participants, Sm infection intensity was predominantly light and positively associated with responses to both motifs. Principal component and hierarchical cluster analysis reduced the data to a set of variables that captured core β-1,2-xylose- and α-1,3-fucose-specific responses, and confirmed associations with Sm and the rural environment. Responses to core β-1,2-xylose and α-1,3-fucose have distinctive relationships with Sm infection and intensity that should further be explored for associations with protective immunity, and cross-reactivity with other exposures.
Highlights
Core β-1,2-xylose and α-1,3-fucose are antigenic motifs on schistosome N-glycans, as well as prominent IgE targets on some plant and insect glycoproteins
We recently reported that community-based intensive versus standard anthelminthic intervention in the rural survey reduced Schistosoma mansoni (Sm) infection intensity but had no effect on the overall Sm prevalence[52]
The current analysis found no evidence of an effect of intensive versus standard treatment on total IgE, soluble egg antigen (SEA)- or SWA-specific antibodies, or on antibody reactivity to any of the N-glycans on the microarray
Summary
Core β-1,2-xylose and α-1,3-fucose are antigenic motifs on schistosome N-glycans, as well as prominent IgE targets on some plant and insect glycoproteins. Analysis of asparagine (N)-linked glycans expressed by schistosomes reveals two standout, non-mammalian substitutions[22,23] on the trimannosyl-chitobiose core (Man3GlcNAc2, conserved in all eukaryotes): an α-1,3-fucose (α3Fuc) linked to the asparagine-linked N-acetylglucosamine (GlcNAc) of the chitobiose component and a β-1,2-xylose (β2Xyl) linked to the β-mannose of the trimannosyl component[24] (Fig. 1) These substitutions are found on nematode glycans from Haemonchus contortus and Caenorhabditis elegans[25,26,27,28], and on invertebrate[29,30] and plant glycans[31,32,33], but have so far not been detected on glycans from other helminths prevalent in the tropics[19]. Whether protective immunity against Schistosoma infection and reinfection (long associated with host IgE responses44,45) can be credited to these epitopes will require further investigations in animal and human studies
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