Protective antibodies to schistosome infections include IgG responses to the core Xyl/Fuc epitopes in surface-expressed N-glycans

A group from Department of Biochemistry, Emory University School of Medicine, Atlanta, GA, USA, etc. has reported that protective antibodies to schistosome infections in brown rats and rhesus monkeys include IgG responses to the core Xyl/Fuc epitopes in surface-expressed N-glycans, and raise the potential of novel glyco-based vaccines that might be developed to combat this disease.
https://pubmed.ncbi.nlm.nih.gov/37081851/

Schistosomiasis, caused by infection with parasitic helminths of the genus Schistosoma, infects over two hundred million people worldwide and causes up to seventy million disability-adjusted-life years (DALYs)—more DALYs than those caused by malaria. Therefore, it is thought that novel vaccine targets are urgently needed. Many different mammals can host schistosomes. Humans become chronically infected, while Rodents can clear the worms soon after infection.

Human N-glycans typically contain a core modification of the GlcNAc residues in GlcNAc-Asn by α6-linked fucose. Core α2-Xylose (CX) and core α3-Fucose (CF) are not found in humans, but are common in N-glycans from insects (CF), plants (CX, CF), and worms (CX, CF).

In ths work, it was demonstrated that antibodies including rabbit anti-horseradish peroxidase (rabαHRP) to CX/CF promote complement-dependent and glycan-specific killing of schistosomula in vitro.