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,
*
Department of Immunology, Osaka Medical Center for Cancer and Cardiovascular Diseases, Higashinari-ku, Osaka, Japan;
Nara Institute of Science and Technology, Ikoma, Nara, Japan;
Organization for Pharmaceutical Safety and Research, Tokyo, Japan;
§
Department of Microbiology, University of Washington School of Medicine, Seattle, WA 98195; and
¶
Department of Neurovirology, Research Institute for Microbial Diseases, Osaka University, Suita, Osaka, Japan
Human CD46, formerly membrane cofactor protein, binds and
inactivates complement C3b and serves as a receptor for measles virus
(MV), thereby protecting cells from homologous complement and
sustaining systemic measles infection. Suppression of cell-mediated
immunity, including down-regulation of IL-12 production, has been
reported on macrophages (M
) by cross-linking their CD46. The
intracellular events responsible for these immune responses, however,
remain unknown. In this study, we found that 6- to 8-day GM-CSF-treated
peripheral blood monocytes acquired the capacity to recruit
protein-tyrosine phosphatase SHP-1 to their CD46 and concomitantly were
able to produce IL-12 p40 and NO. These responses were induced by
stimulation with mAbs F(ab')2 against CD46 that block MV
binding or by a wild-type MV strain Kohno MV strain (KO; UV treated or
untreated) that was reported to induce early phase CD46
down-regulation. Direct ligation of CD46 by these reagents, but not
intracellular MV replication, was required for these cellular
responses. Interestingly, the KO strain failed to replicate in the 6-
to 8-day GM-CSF-cultured M, while other MV strains replicated to
form syncytia under the same conditions. When stimulated with the KO
strain, rapid and transient dissociation of SHP-1 from CD46 was
observed. These and previous results provide strong evidence that CD46
serves as a signal modulatory molecule and that the properties of
ligands determine suppression or activation of an innate immune system
at a specific maturation stage of human M.
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