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Medical Research Council Immunochemistry Unit, Department of Biochemistry, University of Oxford, Oxford, United Kingdom
LFA-1 (CD11a/CD18) and Mac-1 (CD11b/CD18) are members of the
ß2 integrins involved in leukocyte function during immune
and inflammatory responses. We aimed to determine a minimized
ß2 subunit that forms functional LFA-1 and Mac-1. Using a
series of truncated ß2 variants, we showed that the
subregion Q23-D300 of the ß2 subunit is sufficient to
combine with the 
L and M subunits
intracellularly. However, only the ß2 variants
terminating after Q444 promote cell surface expression of LFA-1 and
Mac-1. Thus, the major cysteine-rich region and the three highly
conserved cysteine residues at positions 445, 447, and 449 of the
ß2 subunit are not required for LFA-1 and Mac-1 surface
expression. The surface-expressed LFA-1 variants are constitutively
active with respect to ICAM-1 adhesion and these variants express the
activation reporter epitope of the mAb 24. In contrast,
surface-expressed Mac-1, both the wild type and variants, require 0.5
mM MnCl2 for adhesion to denatured BSA. These results
suggest that the role of the ß2 subunit in LFA-1- and
Mac-1-mediated adhesion may be different.
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