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Monoclonal antibody-defined functional epitopes on the adhesion- promoting
glycoprotein complex (CDw18) of human neutrophils
WJ Wallis, DD Hickstein, BR Schwartz, CH June, HD Ochs, PG Beatty, SJ Klebanoff and JM Harlan
We have evaluated the functional and immunochemical activities of three
monoclonal antibodies (MoAbs) minimally reactive with adherence- defective
neutrophils (PMN) from a patient with recurrent bacterial infections. In
studies with normal PMN, MoAbs OKM1 and 60.1 both precipitate the same
165kd alpha-subunit (alpha M) within an alpha-beta heterodimer complex
(CD11). The CD11 complex is part of a larger complex composed of four
glycoproteins (CDw18) precipitated by MoAb 60.3, with properties suggesting
that the CDw18 complex is equivalent to the Mac-1, LFA-1, p150, 95
glycoprotein family implicated in adherence-dependent leukocyte functions.
PMN adherence to endothelium, spreading on surfaces, aggregation, and
phagocytosis of zymosan particles were all inhibited in a dose-dependent
fashion by MoAb 60.1 (analogous to previous studies with MoAb 60.3) while
MoAb OKM1 had no effect. These findings unify previously disparate
observations and suggest that a functionally active site on the adherence
promoting glycoprotein complexes CD11 and CDw18 is distant from the alpha M
epitope recognized by MoAb OKM1 but closely associated with the alpha M
epitope recognized by MoAb 60.1 and the beta-epitope (or epitope created by
alpha-beta quaternary structure) recognized by MoAb 60.3.
Volume 67,
Issue 4,
pp. 1007-1013,
04/01/1986
Copyright © 1986 by The American Society of Hematology
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