Modification at C6 of the terminal galactosyl residues of cobra venom factor abolishes anti-α-Gal antibody immunoreactivity without affecting functional activity

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Abstract

The N-linked oligosaccharides of cobra venom factor (CVF) contain unique terminal α-galactosylated Lewis X structures. We have previously shown that CVF immobilized on nylon membranes binds naturally occurring human anti-α-Gal antibody. The present study shows that soluble CVF can effectively inhibit the binding of anti-α-Gal antibody to CVF-coated microtiter plates, indicating that the terminal α-galactosyl residues of the functionally active CVF are accessible to anti-α-Gal antibody binding. Modification of the terminal galactosyl residues of CVF by treatment with galactose oxidase and in situ derivatization of the generated aldehyde groups with hydrazides abolished the human anti-α-Gal antibody immunoreactivity without affecting the complement-activating activity.

Original languageEnglish (US)
Pages (from-to)28-32
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume245
Issue number1
DOIs
StatePublished - Apr 7 1998

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Anti-Idiotypic Antibodies
Antibodies
Galactose Oxidase
Nylons
Oligosaccharides
Aldehydes
cobra venom factor
Membranes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

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title = "Modification at C6 of the terminal galactosyl residues of cobra venom factor abolishes anti-α-Gal antibody immunoreactivity without affecting functional activity",
abstract = "The N-linked oligosaccharides of cobra venom factor (CVF) contain unique terminal α-galactosylated Lewis X structures. We have previously shown that CVF immobilized on nylon membranes binds naturally occurring human anti-α-Gal antibody. The present study shows that soluble CVF can effectively inhibit the binding of anti-α-Gal antibody to CVF-coated microtiter plates, indicating that the terminal α-galactosyl residues of the functionally active CVF are accessible to anti-α-Gal antibody binding. Modification of the terminal galactosyl residues of CVF by treatment with galactose oxidase and in situ derivatization of the generated aldehyde groups with hydrazides abolished the human anti-α-Gal antibody immunoreactivity without affecting the complement-activating activity.",
author = "Channe Gowda",
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T1 - Modification at C6 of the terminal galactosyl residues of cobra venom factor abolishes anti-α-Gal antibody immunoreactivity without affecting functional activity

AU - Gowda, Channe

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N2 - The N-linked oligosaccharides of cobra venom factor (CVF) contain unique terminal α-galactosylated Lewis X structures. We have previously shown that CVF immobilized on nylon membranes binds naturally occurring human anti-α-Gal antibody. The present study shows that soluble CVF can effectively inhibit the binding of anti-α-Gal antibody to CVF-coated microtiter plates, indicating that the terminal α-galactosyl residues of the functionally active CVF are accessible to anti-α-Gal antibody binding. Modification of the terminal galactosyl residues of CVF by treatment with galactose oxidase and in situ derivatization of the generated aldehyde groups with hydrazides abolished the human anti-α-Gal antibody immunoreactivity without affecting the complement-activating activity.

AB - The N-linked oligosaccharides of cobra venom factor (CVF) contain unique terminal α-galactosylated Lewis X structures. We have previously shown that CVF immobilized on nylon membranes binds naturally occurring human anti-α-Gal antibody. The present study shows that soluble CVF can effectively inhibit the binding of anti-α-Gal antibody to CVF-coated microtiter plates, indicating that the terminal α-galactosyl residues of the functionally active CVF are accessible to anti-α-Gal antibody binding. Modification of the terminal galactosyl residues of CVF by treatment with galactose oxidase and in situ derivatization of the generated aldehyde groups with hydrazides abolished the human anti-α-Gal antibody immunoreactivity without affecting the complement-activating activity.

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