Direct evidence for a receptor-ligand interaction between the T-cell surface antigen CD2 and lymphocyte-function-associated antigen 3

Journal Article · Thu Oct 01 04:00:00 EDT 1987 · Proc. Natl. Acad. Sci. U.S.A.; (United States)

DOI:https://doi.org/10.1073/pnas.84.19.6864· OSTI ID:7242104

Takai, Y; Reed, M L; Burakoff, S J; Herrmann, S H

The recognition of foreign antigen by T lymphocytes requires direct contact with cells expressing the antigen. It has recently become clear that T lymphocytes can form conjugates with other cells in the absence of foreign antigen expression. Studies using monoclonal antibodies (mAbs) to inhibit conjugate formation have suggested that a portion of the antigen-dependent adhesion is mediated by T lymphocytes interacting with cells expressing lymphocyte-function-associated antigen 3(LFA-3), a widely distributed cell surface protein. The authors have investigated antigen-independent adhesion by incorporating affinity-purified LFA-3 into the lipid membrane of an artificial target cell. These vesicles are similar in size and density to intact cells, so that conjugates between cells and ATCs may be seen by light microscopy. ATCs expressing a density of LFA-3 similar to that on intact cells were found to form conjugates with T cells, but only if the T cells expressed the sheep erythrocyte receptor, CD2 (T11; LFA-2). Previous studies using mAbs have implicated the CD2 molecule in both adhesion and T-cell activation. ATCs prepared without surface protein or with purified HLA class I protein failed to interact with the CD2-positive T cells, indicating that the adhesion found was mediated by the LFA-3 molecule. Furthermore, mAb against LFA-3 or CD2 was able to block the LFA-3-mediated vesicle-cell interaction, whereas mAb against LFA-1 or HLA failed to inhibit the interaction. These results provide direct evidence that LFA-3 functions as an adhesion molecule by serving as a ligand for the D2 molecule on T cells.

• Research Organization: Harvard Medical School, Boston, MA (USA)
• OSTI ID: 7242104
• Journal Information: Proc. Natl. Acad. Sci. U.S.A.; (United States), Journal Name: Proc. Natl. Acad. Sci. U.S.A.; (United States) Vol. 84:19; ISSN PNASA
• Country of Publication: United States
• Language: English

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59 BASIC BIOLOGICAL SCIENCES
62 RADIOLOGY AND NUCLEAR MEDICINE
ANIMAL CELLS
ANIMALS
ANTIBODIES
ANTIGENS
AUTORADIOGRAPHY
BETA DECAY RADIOISOTOPES
BIOLOGICAL MATERIALS
BLOOD
BLOOD CELLS
BODY FLUIDS
CONFIGURATION INTERACTION
CONNECTIVE TISSUE CELLS
DAYS LIVING RADIOISOTOPES
DOMESTIC ANIMALS
ELECTRON CAPTURE RADIOISOTOPES
ERYTHROCYTES
IN VITRO
INTERMEDIATE MASS NUCLEI
IODINE 125
IODINE ISOTOPES
ISOTOPES
LEUKOCYTES
LIGANDS
LYMPHOCYTES
MAMMALS
MAN
MATERIALS
MEMBRANE PROTEINS
MONOCLONAL ANTIBODIES
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
PRIMATES
PROTEINS
PURIFICATION
RADIOISOTOPES
RECEPTORS
RUMINANTS
SHEEP
SOMATIC CELLS
VERTEBRATES