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I and i Antigens of Human Peripheral Blood Lymphocytes Cocap with Receptors for Concanavalin A

T. Feizi, A. Kapadia and W. J. Yount
Proceedings of the National Academy of Sciences of the United States of America
Vol. 77, No. 1, [Part 2: Biological Sciences] (Jan., 1980), pp. 376-380
Stable URL: http://www.jstor.org/stable/8207
Page Count: 5
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I and i Antigens of Human Peripheral Blood Lymphocytes Cocap with Receptors for Concanavalin A
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Abstract

Surface immunofluorescence experiments using a human anti-i and two anti-I antisera have been performed on human peripheral blood lymphocytes. These are known to contain cold-reactive monoclonal IgM antibodies against the carbohydrate sequence: Galβ 1→ 4GlcNAcβ 1→ 3Galβ 1→ 4 GlcNAcβ 1→ 3Gal--(anti-i Den) and the 1→ 4, 1→ 6 domain (anti-I Ma) and the 1→ 4, 1→ 3 domain (anti-I Step) of the branched I-active structure: $\aligned & \text{Gal}\beta 1\rightarrow 4\text{GlcNAc}\beta 1\searrow \\ & \text{Gal}\beta 1\rightarrow 4\text{GlcNAc}\beta 1\nearrow \endaligned {}_{3}^{6}\text{Gal}\beta 1\rightarrow 4\text{GlcNAc}\beta 1\rightarrow 3\text{Gal}$--. A high proportion of B- and T-type lymphocytes express these I and i determinants. In the presence of anti-human immunoglobulin, the cold-reactive membrane-associated complexes of I-anti-I and i-anti-i become stabilized, and redistribution (with patching and capping) can be elicited at 37 degrees C. Dual fluorescence experiments have shown striking concordant staining of I or i (fluorescein) caps and patches with concanavalin A (rhodamine) reactive sites on normal and leukemic cells, suggesting that a proportion of I and i active structures of lymphocyte membranes are structurally associated or physiologically coupled with glycoproteins carrying oligosaccharides with branched mannosyl cores.

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