Glycosylation of the T-cell antigen-specific receptor and its potential role in lectin-mediated cytotoxicity

Journal Article · Sat Mar 01 04:00:00 EST 1986 · Proc. Natl. Acad. Sci. U.S.A.; (United States)

DOI:https://doi.org/10.1073/pnas.83.6.1852· OSTI ID:5877341

Hubbard, S C; Kranz, D M; Longmore, G D; Sitkovsky, M V; Eisen, H N

Cytotoxic T lymphocytes (CTLs) normally destroy only those cells (target cells) whose surface antigens they recognize. However, in the presence of lectins such as Con A, CTLs destroy virtually any cell, regardless of its antigens. The oligosaccharides of the T-cell antigen-specific receptor, a dimeric surface glycoprotein composed of disulfide-linked ..cap alpha.. and ..beta.. subunits, are of interest because of their potential involvement in this lectin-dependent cytotoxic activity. The authors report here that three or four asparagine-linked oligosaccharides could be enzymatically removed from each of the receptor subunits expressed by a cloned line of murine CTLs (clone 2C), consistent with the presence of glycosylation sites deduced from cDNA sequences of the ..cap alpha.. and ..beta.. genes expressed in this clone. All the N-linked glycans on the ..cap alpha.. subunit were of the complex type, but the ..beta.. subunit carried two or three endoglycosidase H-sensitive oligosaccharides. High-mannose glycans can bind tightly to Con A and, indeed, this lectin was found to bind specifically to solubilized 2C T-cell receptor. The Con A-dependent cytotoxic activity of clone 2C, but not of other CTL clones, was inhibited by a monoclonal antibody (1B2) that is specific for the T-cell receptor of clone 2C. Antibody 1B2 also inhibited clone 2C cytotoxicity mediated by phytohemagglutinin, lentil-lectin, and wheat-germ agglutinin. These results suggest that, although lectin-dependent lysis of target cells by CTLs is antigen nonspecific, the cytolytic activity can be triggered by binding of the lectin to the T-cell antigen-specific receptor.

• Research Organization: Massachusetts Institute of Technology, Cambridge
• OSTI ID: 5877341
• Journal Information: Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 83:6; ISSN PNASA
• Country of Publication: United States
• Language: English

Related Subjects

550601* -- Medicine-- Unsealed Radionuclides in Diagnostics
62 RADIOLOGY AND NUCLEAR MEDICINE
ALKALI METAL COMPOUNDS
ANIMAL CELLS
ANIMALS
ANTIGENS
BETA DECAY RADIOISOTOPES
BIOCHEMISTRY
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
CARBOHYDRATES
CHEMISTRY
CONNECTIVE TISSUE CELLS
DAYS LIVING RADIOISOTOPES
ELECTRON CAPTURE RADIOISOTOPES
ELECTROPHORESIS
HALIDES
HALOGEN COMPOUNDS
INORGANIC PHOSPHORS
INTERMEDIATE MASS NUCLEI
IODIDES
IODINE 125
IODINE COMPOUNDS
IODINE ISOTOPES
ISOTOPE APPLICATIONS
ISOTOPES
LECTINS
LEUKOCYTES
LYMPHOCYTES
MAMMALS
MATERIALS
MEMBRANE PROTEINS
MICE
NUCLEI
ODD-EVEN NUCLEI
OLIGOSACCHARIDES
ORGANIC COMPOUNDS
PHOSPHORS
PROTEINS
RADIOISOTOPES
RADIORECEPTOR ASSAY
RECEPTORS
RODENTS
SACCHARIDES
SODIUM COMPOUNDS
SODIUM IODIDES
SOMATIC CELLS
TOXICITY
TRACER TECHNIQUES
VERTEBRATES