COVALENT BINDING OF NON-PROTEOLYSED C3 TO JURKAT T-CELLS

Purified C3 binds covalently to Jurkat T cells upon incubation at neutral pH. This binding does not appear to involve proteolysis of C3; it leads to high-molecular-weight associations, preferentially through ester linkages, which are disrupted upon incubation with hydroxylamine at alkaline pH. Part of the association also appears to involve disulfide links between C3 and Jurkat cells. Similarly, plasma membranes purified from these cells bind C3 with no evidence for proteolysis of C3. Binding of C3 appears to be "catalysed" by Jurkat cells, and is not due to the well-known spontaneous hydrolysis of C3. Binding of C3 involves hydrolysis of its thioester bond, as titratable-SH groups are available in soluble C3 after incubation of purified C3 with Jurkat plasma membranes; loss of C3 haemolytic activity confirms this finding. These observations give evidence for the binding of C3b-like C3 to Jurkat cells, conferring on these cells the potential to interact with other complement receptor-bearing cells such as B cells.