Multiple ICAM-1 (CD54) epitopes are involved in homotypic B-cell adhesion.

Abstract:

: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 1 (ICAM-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 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 homotypic B-cell adhesion of cell line ML1.

journal_name

Scand J Immunol

authors

Bloemen P,Moldenhauer G,van Dijk M,Schuurman HJ,Bloem AC

doi

10.1111/j.1365-3083.1992.tb03250.x

keywords:

subject

Has Abstract

pub_date

1992-05-01 00:00:00

pages

517-23

issue

5

eissn

0300-9475

issn

1365-3083

journal_volume

35

pub_type

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