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The complement system membrane cofactor protein (MCP) CD46
serves as a C3b/C4b inactivating factor for the protection of host
cells from autologous complement attack and as a receptor for measles
virus (MV). MCP consists of four short consensus repeats (SCR) which
are the predominant extracellular structural motif. In the present
study, we determined which of the four SCR of MCP contribute to its
function using Chinese hamster ovary cell clones expressing each SCR
deletion mutants. The results were as follows: 1) SCR1 and SCR2 are
mainly involved in MV binding and infection; 2) SCR2, SCR3, and SCR4
contribute to protect Chinese hamster ovary cells from human
alternative complement pathway-mediated cytolysis; and 3) SCR2 and SCR3
are essential for protection of host cells from the classical
complement pathway. These results on cell protective activity of the
mutants against the human classical and the alternative complement
pathways were compatible with factor I-mediated inactivation profiles
of C4b and C3b, respectively, in the fluid-phase assay using
solubilized mutants and factor I; the results were mostly consistent
with those reported by Adams et al. (Adams, E. M., Brown, M.
C., Nunge, M., Krych, M., and Atkinson, J. P.(1991) J. Immunol. 147, 3005-3011). SCR2 and SCR3 were required for C3b and C4b
inactivation, and SCR4-deleted MCP showed weak cofactor activity for
C4b cleavage but virtually no cofactor activity for C3b cleavage. The
functional domains of MCP for the three natural ligands C3b, C4b, and
MV, therefore, map to different, although partly overlapping, SCR
domains.
Volume 270,
Number 25,
Issue of June 23, pp. 15148-15152, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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