Lectin-dependent inhibition of antigen-antibody reaction: application for measuring α2,6-sialylated glycoforms of transferrin

J Biochem. 2013 Sep;154(3):229-32. doi: 10.1093/jb/mvt065. Epub 2013 Aug 6.

Abstract

We developed a high-throughput Enzyme-linked immunosorbent assay (ELISA) for measuring α2,6-sialylated transferrin (Tf), based on inhibition of anti-Tf antibody binding to α2,6-sialylated Tf by a lectin, Sambucus sieboldiana Agglutinin (SSA). The inhibition was not observed with other glycoforms, such as periodate-treated, sialidase-treated and sialidase/galactosidase-treated Tf, suggesting that the assay was glycoform specific. This finding was applied to an automated latex-agglutination immunoassay, using SSA lectin as an inhibitor (SSA-ALI). The concentration of α2,6-sialylated Tf measured by SSA-ALI in human cerebrospinal fluid was correlated with that of ELISA (r2 = 0.8554), previously developed for measuring α2,6-sialylated Tf.

Keywords: Sambucus sieboldiana Agglutinin lectin; automated latex-agglutination immunoassay; transferring; α2,6-sialic acid.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antigen-Antibody Reactions / immunology*
  • Binding, Competitive
  • Enzyme-Linked Immunosorbent Assay / methods*
  • Glycoproteins / cerebrospinal fluid*
  • Glycosylation
  • Goats
  • High-Throughput Screening Assays
  • Humans
  • Neuraminidase / chemistry
  • Plant Lectins / chemistry*
  • Plant Lectins / immunology
  • Protein Binding
  • Rabbits
  • Ribosome Inactivating Proteins / chemistry*
  • Ribosome Inactivating Proteins / immunology
  • Transferrin / cerebrospinal fluid*

Substances

  • Glycoproteins
  • Plant Lectins
  • Sambucus nigra lectins
  • Transferrin
  • Neuraminidase
  • Ribosome Inactivating Proteins