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Monoclonal Antibodies against Leucoagglutinin‐Reactive Human T‐Lymphocyte Surface Components
Author(s) -
HAMMARSTRÖM M.L.,
BERZINS T.,
AGUILARSANTELISES M.,
ANDERSSON G.,
PERLMANN P.,
HAMMARSTRÖM S.
Publication year - 1988
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1988.tb01510.x
Subject(s) - monoclonal antibody , microbiology and biotechnology , antigen , t cell , t lymphocyte , antibody , lectin , lymphocyte , biology , epitope , concanavalin a , receptor , chemistry , biochemistry , immunology , immune system , in vitro
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 peripheral 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. K‐46M immunoprecipitated 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.