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A unique natural human IgG antibody with anti-alpha-galactosyl specificity.
Abstract
A new natural anti-alpha-galactosyl IgG antibody (anti-Gal) was found to be present in high titer in the serum of every normal individual studied. The antibody was isolated by affinity chromatography on a melibiose-Sepharose column. The reactivity of the antibody was assessed by its interaction with alpha-galactosyl residues on rabbit erythrocytes (RabRBC). The specificity was determined by inhibition experiments with various carbohydrates. The anti-Gal interacts with alpha-galactosyl residues, possibly on glycolipids of human RBC (HuRBC), after removal of membrane proteins by treatment with pronase. In addition, the anti-Gal bind specifically to normal and pathologically senescent HuRBC, suggesting a physiological role for this natural antibody in the aging of RBC. The ubiquitous presence of anti-Gal in high titers throughout life implies a constant antigenic stimulation. In addition to the theoretical interest in the antibody, the study of the anti-Gal reactivity seems to bear immunodiagnostic significance. Decrease in the antibody titer was found to reflect humoral immunodeficiency disorders.
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After birth, humans develop antibodies to α-Gal and Neu5Gc, referred to as preformed antibodies, upon exposure to molecular mimics of these two antigens.
“After birth, humans develop antibodies to α-Gal and Neu5Gc, referred to as preformed antibodies, upon exposure to molecular mimics of these two antigens16,20,21.”
From Design and testing of a humanized porcine donor for xenotransplantation (2023) · cites this paper as [20]
The age-group results (page not supplied) show anti-Gal titers rising after infancy, and the discussion (page not supplied) suggests intestinal bacteria may provide antigenic stimulation. The paper does not address Neu5Gc, and it proposes rather than establishes exposure to bacterial α-Gal as the cause of antibody development. (LLM, conf=0.87)
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Barclay, A. N., & van den Berg, T. K. (2014) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032713-120142 · Cited by 841
Thall, A. D., Malý, P., & Lowe, J. B. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.37.21437 · Cited by 401
Design and testing of a humanized porcine donor for xenotransplantation
Anand, R. P., Layer, J. V., Heja, D., Hirose, T., Lassiter, G., Firl, D. J., Paragas, V. B., Akkad, A., Chhangawala, S., Colvin, R. B., et al. (2023) · Nature · doi:10.1038/s41586-023-06594-4 · Cited by 302
Therapeutic glycoprotein production in mammalian cells
Lalonde, M.-E., & Durocher, Y. (2017) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2017.04.028 · Cited by 296
The α-gal epitope (Galα1-3Galβ1-4GlcNAc-R) in xenotransplantation
Galili, U. (2001) · Biochimie · doi:10.1016/s0300-9084(01)01294-9 · Cited by 212
Self-citationKay, M. M., Bosman, G. J., Shapiro, S. S., Bendich, A., & Bassel, P. S. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.8.2463 · Cited by 130
The Possible Role of Anti-Neu5Gc as an Obstacle in Xenotransplantation
Tector, A. J., Mosser, M., Tector, M., & Bach, J.-M. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00622 · Cited by 60
Mateos-Hernández, L., Risco-Castillo, V., Torres-Maravilla, E., Bermúdez-Humarán, L. G., Alberdi, P., Hodžić, A., Hernández-Jarguin, A., Rakotobe, S., Galon, C., Devillers, E., et al. (2020) · Vaccines · doi:10.3390/vaccines8020285 · Cited by 46
Modifying the sugar icing on the transplantation cake
Cooper, D. K. C. (2016) · Glycobiology · doi:10.1093/glycob/cww028 · Cited by 36
Stone, K. R., Walgenbach, A., & Galili, U. (2017) · Tissue Engineering Part B: Reviews · doi:10.1089/ten.teb.2016.0332 · Cited by 22
Self-citationGasek, N., Dearborn, J., Enes, S. R., Pouliot, R., Louie, J., Phillips, Z., Wrenn, S., Uhl, F. E., Riveron, A., Bianchi, J., et al. (2021) · Biomaterials · doi:10.1016/j.biomaterials.2021.121029 · Cited by 16
Metadata
- Authors
- Galili, U., Rachmilewitz, E. A., Peleg, A., & Flechner, I.
- Venue
- The Journal of experimental medicine
- Publisher
- Rockefeller University Press
- Published
- 1984-11-01
- Volume
- 160
- Issue
- 5
- Pages
- 1519-1531
- ISSN
- 0022-1007
- 1540-9538
- PMC
- PMC2187506
- Cited by
- 631
- References
- 0
- Language
- en
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