Preparation and specificities of antisera to β1 → 4 linked n-acetyl-D-glucosamine oligosaccharides

Anderas, Per R.; Paul, Deepika; Tomita, Joseph T.; Anderson, Byron

doi:10.1016/0161-5890(79)90136-6

Cited by 11 publications

(1 citation statement)

References 12 publications

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“…The αGal trisaccharide epitope sequences Galα1,3Galβ1,4Gal and Galα1,3Galβ1,4GlcNAc, purchased from V Labs (Covington, LA, USA), were conjugated to ovalbumin (Sigma, St Louis, MO, USA) by reductive amination with NaCNBH 3 (Sigma) [29]. Using the phenol–sulfuric acid method for neutral sugar quantitation [30] and αGal as a standard, 8–10 trisaccharides were found to be coupled per ovalbumin molecule.…”

Section: Methodsmentioning

confidence: 99%

IgY antiporcine endothelial cell antibodies effectively block human antiporcine xenoantibody binding

Fryer

Firca²,

Leventhal

et al. 1999

Xenotransplantation

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Avian IgY antibodies are structurally different from mammalian IgGs and do not fix mammalian complement components or bind human Fc receptors. As these antibody-mediated interactions are believed to play significant roles in both hyperacute rejection (HAR) and acute vascular xenograft rejection (AVXR), IgY antibodies to xenoantigen target epitopes may inhibit these rejection processes. In this report, we show that chicken IgY antibodies to alpha-Gal antigen epitopes and to other porcine aortic endothelial cell (PAEC) antigens block human xenoreactive natural antibody binding to both porcine and rat cardiac tissues and porcine kidney tissues. Chicken IgY antibodies blocked complement-mediated lysis of PAECs by human serum, and inhibited antibody-dependent cell-mediated lysis of PAECs by heat-inactivated human serum plus peripheral blood leukocytes. Binding of IgY to porcine endothelial cells did not affect cell morphology nor expression of E-selectin. These results suggest that avian IgYs could be of potential use in inhibiting pig-to-human xenograft rejection.

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Section: Methodsmentioning

confidence: 99%