Specificity of xenoreactive anti-Galα1–3Gal IgM for α-galactosyl ligands

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Abstract
The transplantation of organs from lower animals such as pigs into humans is prevented by a severe rejection reaction initiated by complement fixing xenoreactive natural antibodies. Most anti-pig xenoreactive natural antibodies in humans are thought to recognize Galα1-3Galαβ1-4GlcNAc and are also thought to recognize, albeit less avidly, Galα1-6Glc. Galα-6Glc has been used as a ligand for purification of ‘anti-Galα1-3Gal antibodies’ and as a therapeutic or reagent to prevent the binding of these antibodies to porcine organs or cells. We tested the specificity of anti-Galα1-3Gal IgM for Galα1-6Glc and related saccharides. Based on inhibition of binding of xenoreactive anti-Galα1-3Gal IgM to porcine cells by soluble saccharides, anti-Galα1-3Gal IgM in a human serum was found to consist of a mixture of antibodies which have a similar affinity for Galα1-3Gal but varying affinities for Galαl-6Glc and other structures. Twenty to 40% of the anti-Galα1-3Gal IgM from the population tested did not recognize Galα1-6Glc. The binding of anti-Galα1-3Gal IgM to Galα1-6Glc varied widely from individual to individual, some samples lacking almost entirely anti-Galα1-3Gal IgM which bound to Galα1-6Glc.

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