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- Title
Monoclonal Antibodies against Leucoagglutinin- Reactive Human T-Lymphocyte Surface Components I. Characterization of Cellular Binding Sites.
- Authors
Hammarström, M.-L.; Berzins, T.; Aguilar-Santelises, M.; Andersoon, G.; Perlmann, P.; Hammarström, S.
- Abstract
The binding specificities of three biologically active anti-lymphocyte monoclonal antibodies (MoAb) (K46M, K3G, and 3–19–2) produced against human T-cell surface components reactive with the mitogenic lectin leucoagglutinin from Phaseolus vulgaris (La) were analysed. K46M is a strong T-cell mitogen, while K3G and 3–19–2 inhibited cell-mediated cytotoxicity. Resting periphera1 blood lymphocytes (PBL) contained 4–16% K46M+ cells. 8–35% K3G+ cells, and <0.3–4% 3–19–2+ cells. After stimulation with T-cell mitogens the proportion of K46M+ and 3–19–2+ cells increased markedly (mean 59 and 30% positive cells, respectively), while the increase in K3G+ cells was less prominent (38%). K46M-reactive structures were expressed on mature T cells and probably also on B cells. K3G reacted with B and T cells while 3–19–2 showed a broader specificity reacting also with erythrocytes. All three MoAb reacted with lipid extracts of resting and activated PBL as well as with purified neutral glycolipids of lymphoid origin. In addition 3–19–2 reacted with lipid extracts of erythrocytes. K46M immuno- precipitated four surface peptides from lectin-stimulated PBL. Their apparent molecular weights were 53,000, 42,000, and 16,000 (doublet). The 53,000 and 42,000 MW peptides were identified as the α and β chains of the T-cell antigen receptor. The identity of the 16,000 MW peptides is presently unknown. K3G and 3–19–2 did not specifically precipitate any lymphocyte surface peptide.
- Subjects
IMMUNOSPECIFICITY; MONOCLONAL antibodies; T cells; MITOGENS; LEUCOAGGLUTININS; BINDING sites; CELL membranes; IMMUNOLOGY
- Publication
Scandinavian Journal of Immunology, 1988, Vol 28, Issue 6, p759
- ISSN
0300-9475
- Publication type
Article
- DOI
10.1111/j.1365-3083.1988.tb01510.x