High affinity binding of the Entamoeba histolytica lectin to polyvalent N-acetylgalactosaminides.

@article{Adler1995HighAB,
  title={High affinity binding of the Entamoeba histolytica lectin to polyvalent N-acetylgalactosaminides.},
  author={Pablo Adler and Stephen J. Wood and Young Choon Lee and Reiko T. Lee and William A Petri and Ronald L. Schnaar},
  journal={The Journal of biological chemistry},
  year={1995},
  volume={270 10},
  pages={5164-71}
}
Entamoeba histolytica trophozoites initiate pathogenic colonization by adherence to host glycoconjugates via an amebic surface lectin which binds to galactose (Gal) and N-acetylgalactosamine (GalNAc) residues. Monovalent and multivalent carbohydrate ligands were screened for inhibition of E. histolytica lectin-mediated human red cell hemagglutination, revealing that: (i) the synthetic multivalent neoglycoprotein GalNAc39BSA (having an average of 39 GalNAc residues linked to bovine serum albumin… CONTINUE READING

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