Journal of Experimental Medicine, Vol 144, 1695-1700, Copyright © 1976 by Rockefeller University Press
Concanavalin A-mediated binding and sphering of human red blood cells by homologous monocytes
D Guerry, MA Kenna, AD Schrieber and RA Cooper
Human red blood cells sensitized with concanavalin A became bound to
homologous peripheral blood monocytes. Binding occured at a concentration
of 10(5) molecules of tetrameric Con A per red blood cell (RBC) and
increased with additional Con A. RBC binding began within 5 min and was
maximal at 90 min. Phagocytosis of sensitized RBCs was minimal. RBC
attachment was prevented by 0.01 M alpha-methyl-D- mannopyranoside, and,
once the RBC-monocyte rosette was established, bound RBCs were largely
removed with this specific saccharide inhibitor of Con A. RBCs attached to
monocytes became spherocytic and osmotically fragile. The recognition of
concanavalin A (Con A)-coated RBCs was not mediated through the monocyte
IgG-Fc receptor. These studies demonstrate that, like IgG and C3b, Con A is
capable of mediating the binding of human RBCs to human monocytes. Red
cells so bound are damaged at the monocyte surface.
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