Diversity in specificity, abundance, and composition of anti-Neu5Gc antibodies in normal humans: potential implications for disease.

@article{PadlerKaravani2008DiversityIS,
  title={Diversity in specificity, abundance, and composition of anti-Neu5Gc antibodies in normal humans: potential implications for disease.},
  author={Vered Padler-Karavani and Hai Yu and Hongzhi Cao and Harshal A. Chokhawala and Felix Karp and Nissi M. Varki and Xin Chen and Ajit Varki},
  journal={Glycobiology},
  year={2008},
  volume={18 10},
  pages={818-30}
}
Human heterophile antibodies that agglutinate animal erythrocytes are known to detect the nonhuman sialic acid N-glycolylneuraminic acid (Neu5Gc). This monosaccharide cannot by itself fill the binding site (paratope) of an antibody and can also be modified and presented in various linkages, on diverse underlying glycans. Thus, we hypothesized that the human anti-Neu5Gc antibody response is diverse and polyclonal. Here, we use a novel set of natural and chemoenzymatically synthesized glycans to… CONTINUE READING
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