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Biophysical characteristics of anti-Gal(alpha)1-3Gal IgM binding to cell surfaces: implications for xenotransplantation.

Publication ,  Journal Article
Parker, W; Stitzenberg, KB; Yu, PB; Pratt, VS; Nakamura, YC; Farel, LS; Ward, CM; Lin, SS; Everett, ML; Platt, JL
Published in: Transplantation
February 15, 2001

BACKGROUND: Natural antibodies directed against cell surface carbohydrates are thought to be vital to host defense and to initiate the rejection of xenografts and ABO-incompatible allografts. The biophysical properties underlying the association and dissociation of these antibodies from cell surfaces is incompletely understood. We investigated those properties for the binding of Galalpha1-3Gal antibodies to porcine endothelial cell surfaces, because such interactions might be relevant to the clinical application of xenotransplantation. RESULTS AND CONCLUSIONS: The initial rate of binding of anti-Galalpha1-3Gal antibodies to endothelial cells was found to depend on antibody concentration, antibody diffusion, and antigen concentration. The presence of an intact glycocalyx had a greater impact on antibody binding than mobility of antigen in cell membranes. Disruption of glycocalyx increased the amount of antibody bound at equilibrium by more than 50%. Although the binding of anti-Galalpha1-3Gal antibodies to cell surfaces could be inhibited by soluble Galalpha1-3Gal, once bound, some anti-Galalpha1-3Gal could not be dissociated by competitive inhibitors of binding or by denaturation of the bound Ig with chaotropic reagents, but could be dissociated by reduction of disulfide bonds, suggesting that attachment to cell surfaces was, at least in part, by means other than specific reaction with the epitope.

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Published In

Transplantation

DOI

ISSN

0041-1337

Publication Date

February 15, 2001

Volume

71

Issue

3

Start / End Page

440 / 446

Location

United States

Related Subject Headings

  • Viscosity
  • Transplantation, Heterologous
  • Temperature
  • Swine
  • Surgery
  • Sensitivity and Specificity
  • Protein Binding
  • Humans
  • Glycocalyx
  • Epitopes
 

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Parker, W., Stitzenberg, K. B., Yu, P. B., Pratt, V. S., Nakamura, Y. C., Farel, L. S., … Platt, J. L. (2001). Biophysical characteristics of anti-Gal(alpha)1-3Gal IgM binding to cell surfaces: implications for xenotransplantation. Transplantation, 71(3), 440–446. https://doi.org/10.1097/00007890-200102150-00018
Parker, W., K. B. Stitzenberg, P. B. Yu, V. S. Pratt, Y. C. Nakamura, L. S. Farel, C. M. Ward, S. S. Lin, M. L. Everett, and J. L. Platt. “Biophysical characteristics of anti-Gal(alpha)1-3Gal IgM binding to cell surfaces: implications for xenotransplantation.Transplantation 71, no. 3 (February 15, 2001): 440–46. https://doi.org/10.1097/00007890-200102150-00018.
Parker W, Stitzenberg KB, Yu PB, Pratt VS, Nakamura YC, Farel LS, et al. Biophysical characteristics of anti-Gal(alpha)1-3Gal IgM binding to cell surfaces: implications for xenotransplantation. Transplantation. 2001 Feb 15;71(3):440–6.
Parker, W., et al. “Biophysical characteristics of anti-Gal(alpha)1-3Gal IgM binding to cell surfaces: implications for xenotransplantation.Transplantation, vol. 71, no. 3, Feb. 2001, pp. 440–46. Pubmed, doi:10.1097/00007890-200102150-00018.
Parker W, Stitzenberg KB, Yu PB, Pratt VS, Nakamura YC, Farel LS, Ward CM, Lin SS, Everett ML, Platt JL. Biophysical characteristics of anti-Gal(alpha)1-3Gal IgM binding to cell surfaces: implications for xenotransplantation. Transplantation. 2001 Feb 15;71(3):440–446.

Published In

Transplantation

DOI

ISSN

0041-1337

Publication Date

February 15, 2001

Volume

71

Issue

3

Start / End Page

440 / 446

Location

United States

Related Subject Headings

  • Viscosity
  • Transplantation, Heterologous
  • Temperature
  • Swine
  • Surgery
  • Sensitivity and Specificity
  • Protein Binding
  • Humans
  • Glycocalyx
  • Epitopes