|
|
||||||||
The Journal of Immunology, Vol 142, Issue 8 2828-2834, Copyright © 1989 by American Association of Immunologists
ARTICLES |
JL Avila, M Rojas and U Galili
Instituto de Biomedicina, Caracas, Venezuela.
Anti-Gal is a natural antibody present in unusually high concentrations in human sera. It constitutes as much as 1% of circulating IgG and displays a distinct specificity for the Gal alpha 1----3Gal carbohydrate epitope. In the present study, we have found in the sera of patients with Chagas' disease and Leishmania infection anti-Gal titers 10- and 16-fold higher than that of healthy or bacteria-infected individuals. This increase in anti-Gal titer seemed to be the result of a specific immune response toward parasitic Gal alpha 1----3Gal epitopes. Binding studies of affinity chromatography-purified anti-Gal antibodies to Trypanosoma cruzi and American Leishmania parasites indeed demonstrated the presence of Gal alpha 1----3Gal epitopes on these parasites. This finding was supported by the observed binding to the parasites of two additional Gal alpha 1----3Gal recognizing molecules: the mAb Gal-13, and the lectin, Bandeiraea simplicifolia I B4. Furthermore, the binding of both anti-Gal antibody and of the B. simplicifolia I B4 lectin could be inhibited by galactose, and not glucose. In addition, removal of the terminal alpha-galactosyl residues from the parasites by pretreatment with alpha-galactosidase, or the oxidation of the binding epitopes by periodate prevented the subsequent binding of both the antibody and the lectin. A crude leishmanial lipid extract readily bound these three reagents, suggesting that at least part of these epitopes are of a glycolipid nature. These Gal alpha 1---- 3Gal epitopes may thus serve as an antigenic source for the excess production of anti-Gal. In view of the naturally high level of anti-Gal in humans and its binding to T. cruzi and Leishmania, it is argued that these antibodies may contribute to the natural defense against the invasion of such parasites.
This article has been cited by other articles:
![]() |
G. H. Hansen, L.-L. Niels-Christiansen, L. Immerdal, and E. M. Danielsen Antibodies in the small intestine: mucosal synthesis and deposition of anti-glycosyl IgA, IgM, and IgG in the enterocyte brush border Am J Physiol Gastrointest Liver Physiol, July 1, 2006; 291(1): G82 - G90. [Abstract] [Full Text] [PDF] |
||||
![]() |
G. H. Hansen, E. D. K. Pedersen, L. Immerdal, L.-L. Niels-Christiansen, and E. M. Danielsen Anti-glycosyl antibodies in lipid rafts of the enterocyte brush border: a possible host defense against pathogens Am J Physiol Gastrointest Liver Physiol, December 1, 2005; 289(6): G1100 - G1107. [Abstract] [Full Text] [PDF] |
||||
![]() |
Y. Zhang, A. Deshpande, Z. Xie, R. Natesh, K. R. Acharya, and K. Brew Roles of active site tryptophans in substrate binding and catalysis by {alpha}-1,3 galactosyltransferase Glycobiology, December 1, 2004; 14(12): 1295 - 1302. [Abstract] [Full Text] [PDF] |
||||
![]() |
K. J. Posekany, H. K. Pittman, J. F. Bradfield, C. E. Haisch, and K. M. Verbanac 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., November 1, 2002; 70(11): 6215 - 6222. [Abstract] [Full Text] [PDF] |
||||
![]() |
V. Pereira-Chioccola, A Acosta-Serrano, I Correia de Almeida, M. Ferguson, T Souto-Padron, M. Rodrigues, L. Travassos, and S Schenkman Mucin-like molecules form a negatively charged coat that protects Trypanosoma cruzi trypomastigotes from killing by human anti-alpha-galactosyl antibodies J. Cell Sci., January 4, 2000; 113(7): 1299 - 1307. [Abstract] [PDF] |
||||
![]() |
M. Dominguez and A. Torano Immune Adherence-mediated Opsonophagocytosis: The Mechanism of Leishmania Infection J. Exp. Med., January 4, 1999; 189(1): 25 - 35. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |