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Multiple ICAM‐1 (CD54) Epitopes are Involved in Homotypic B‐Cell Adhesion
Author(s) -
BLOEMEN P,
MOLDRNHAUER G.,
DIJK M.,
SCHUURMAN H.J.,
BLOEM A. C.
Publication year - 1992
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.1365-3083.1992.tb03250.x
Subject(s) - epitope , monoclonal antibody , glycosylation , cell adhesion molecule , cell adhesion , microbiology and biotechnology , intercellular adhesion molecule 1 , icam 1 , linear epitope , adhesion , chemistry , biology , antibody , biochemistry , cell , immunology , organic chemistry
Two monoclonal antibodies (MoAbs), F10.2 and F10.3. were selected for their ability to interfere in homotypic adhesion of human B cells Precipitation studies and binding to intercellular adhesion molecule I(CAM‐1, CD54) cDNA transfected COS cells revealed that both MoAbs are directed against ICAM‐1. The binding of MoAb F10.2 was inhibited by LB‐2, a MoAb recognizing the NH2‐terminal immunoglobulin‐like domain of ICAM‐1. This suggests that the epitope recognized by F10.2 is located on the first domain of the ICAM‐1. This suggests that the epitope recognized by F10.2 is located on the first domain of the ICAM‐1 molecule. Binding of the other MoAb. F10.3, was not inhibited by F10.2 nor by two other MoAbs mapping to the first domain of the ICAM‐1 molecule. The ability of F10.3 to bind to ICAM‐1 is influenced by glycosylation, suggesting that this epitope is located on one of the domains carrying possible glycosylation sites, i.e. domain 2,3 or 4. The ICAM‐1 epitopes recognized by F10.3 and LB‐2 or F10.2 co‐operated in homotypic adhesion of cells from the EBV cell line ML1. These results suggest that in addition to an epitope located on domain 1 of the ICAM‐1 molecule, another epitope whose exposure can be regulated by glycosylation is involved in homotype B‐cell adhesion of cell line ML1.