The human natural anti-Gal IgG. III. The subtlety of immune tolerance in man as demonstrated by crossreactivity between natural anti-Gal and anti-B antibodies

doi:10.1084/jem.165.3.693

This Article

	Full Text (PDF)
	Alert me when this article is cited
	Citation Map

Services

	Email this article
	Similar articles in this journal
	Similar articles in PubMed
	Alert me to new content in the JEM
	Download to citation manager

Citing Articles

	Citing Articles via HighWire
	Citing Articles via CrossRef
	Citing Articles via Google Scholar

Google Scholar

	Articles by Galili, U.
	Articles by Macher, B. A.
	Search for Related Content

PubMed

	PubMed Citation
	Articles by Galili, U.
	Articles by Macher, B. A.


Social Bookmarking

	What's this?

ARTICLES

The human natural anti-Gal IgG. III. The subtlety of immune tolerance in man as demonstrated by crossreactivity between natural anti-Gal and anti-B antibodies

U Galili, J Buehler, SB Shohet and BA Macher

A well-defined antigen/antibody system was used to evaluate the effect of immune tolerance on the spectrum of specificities of natural antibodies. The antibody used in this study, anti-Gal, is a naturally occurring, polyclonal IgG that constitutes 1% of the circulating IgG in humans. We have previously shown that anti-Gal, purified from AB sera, specifically interacts with glycosphingolipids bearing a Gal alpha 1---- 3Gal epitope, but not with the closely related B antigen in which the penultimate galactose of the Gal alpha 1----3Gal epitope is fucosylated Gal alpha 1----3(Fuc alpha 1----2)Gal. This narrow specificity was assumed to be the result of an effective immune tolerance mechanism that prevents the expression of antibody clones that can recognize both the Gal alpha 1----3Gal and the self B epitopes. If the assumption that immune tolerance determines the range of anti-Gal specificity is correct, then anti-Gal from individuals lacking the B antigen (A and O blood types) would be expected to interact with both Gal alpha 1---- 3Gal and Gal alpha 1----3(Fuc alpha 1----2)Gal epitopes. In this study, anti-Gal from the serum of individuals of various blood types was purified by affinity chromatography on Gal alpha 1----3Gal adsorbent and tested for its reaction with the B antigen. Whereas anti-Gal from AB and B individuals only reacted with Gal alpha 1----3Gal epitopes, anti-Gal from A and O individuals reacted with both Gal alpha 1----3Gal and B epitopes. Furthermore, it was determined that the majority of anti-B reactivity in A and O individuals is in fact anti-Gal antibodies capable of recognizing both Gal alpha 1----3Gal and B epitopes. It can be concluded from these results that immune tolerance accurately controls the spectrum of natural antibody specificities by preventing the production of antibody clones that can interact with self antigens.
Add to CiteULike CiteULike Add to Complore Complore Add to Connotea Connotea Add to Del.icio.us Del.icio.us Add to Digg Digg Add to Reddit Reddit Add to Technorati Technorati What's this?

This article has been cited by other articles:

Abdel-Motal, U. M., Guay, H. M., Wigglesworth, K., Welsh, R. M., Galili, U. (2007). Immunogenicity of Influenza Virus Vaccine Is Increased by Anti-Gal-Mediated Targeting to Antigen-Presenting Cells. J. Virol. 81: 9131-9141 [Abstract] [Full Text]
Mohiuddin, M. M., Ogawa, H., Yin, D.-P., Galili, U. (2003). Tolerance induction to a mammalian blood group--like carbohydrate antigen by syngeneic lymphocytes expressing the antigen, II: tolerance induction on memory B cells. Blood 102: 229-236 [Abstract] [Full Text]
Ogawa, H., Yin, D.-P., Shen, J., Galili, U. (2003). Tolerance induction to a mammalian blood group-like carbohydrate antigen by syngeneic lymphocytes expressing the antigen. Blood 101: 2318-2320 [Abstract] [Full Text]
Posekany, K. J., Pittman, H. K., Bradfield, J. F., Haisch, C. E., Verbanac, K. M. (2002). Induction of Cytolytic Anti-Gal Antibodies in {alpha}-1,3-Galactosyltransferase Gene Knockout Mice by Oral Inoculation with Escherichia coli O86:B7 Bacteria. Infect. Immun. 70: 6215-6222 [Abstract] [Full Text]
Vetere, A., Donati, I., Campa, C., Semeraro, S., Gamini, A., Paoletti, S. (2002). Synthesis and characterization of a novel glycopolymer with protective activity toward human anti-{alpha}-Gal antibodies. Glycobiology 12: 283-290 [Abstract] [Full Text]
Deriy, L., Chen, Z.-c., Gao, G.-P., Galili, U. (2002). Expression of {alpha}-gal epitopes on HeLa cells transduced with adenovirus containing {alpha}1,3galactosyltransferase cDNA. Glycobiology 12: 135-144 [Abstract] [Full Text]
Gowda, D. C., Glushka, J., Halbeek, H. v., Thotakura, R. N., Bredehorst, R., Vogel, C.-W. (2001). N-linked oligosaccharides of cobra venom factor contain novel {{alpha}}(1-3)galactosylated Lex structures. Glycobiology 11: 195-208 [Abstract] [Full Text]
Chiou, S.-T., Chen, Y.-W., Chen, S.-C., Chao, C.-F., Liu, T.-Y. (2000). Isolation and Characterization of Proteins That Bind to Galactose, Lipopolysaccharide of Escherichia coli, and Protein A of Staphylococcus aureus from the Hemolymph of Tachypleus tridentatus. J. Biol. Chem. 275: 1630-1634 [Abstract] [Full Text]
LaTemple, D. C., Abrams, J. T., Zhang, S. Y., Galili, U. (1999). Increased Immunogenicity of Tumor Vaccines Complexed with Anti-Gal: Studies in Knockout Mice for {{alpha}}1,3Galactosyltransferase. Cancer Res. 59: 3417-3423 [Abstract] [Full Text]
Lopez, M., Gazon, M., Juliant, S., Plancke, Y., Leroy, Y., Strecker, G., Cartron, J.-P., Bailly, P., Cerutti, M., Verbert, A., Delannoy, P. (1998). Characterization of a UDP-Gal:Galbeta 1-3GalNAc alpha 1,4-Galactosyltransferase Activity in a Mamestra brassicae Cell Line. J. Biol. Chem. 273: 33644-33651 [Abstract] [Full Text]