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The Journal of Immunology, Vol 143, Issue 12 4117-4122, Copyright © 1989 by American Association of Immunologists
ARTICLES |
L Shen, R Lasser and MW Fanger
Department of Microbiology, Dartmouth Medical School, Hanover, NH 03756.
A mAb My 43 of the IgM isotype was obtained from a fusion of spleen cells immunized against human monocytes. This mAb inhibited monocyte binding of both soluble FITC-labeled IgA and IgA-coated E, whereas it did not inhibit IgG binding. The Ag recognized by My 43 was induced on HL-60 cells in parallel with IgA binding ability by 1-25 dihydroxy- vitamin D3 treatment. Phagocytosis of IgA-coated E by monocytes and 1- 25 dihydroxyvitamin D3-treated HL-60 cells was inhibited by My 43. Furthermore, a heteroantibody of My 43 x F(ab)'2 anti-E promoted phagocytic uptake of E by monocytes. Production of superoxide anion by IFN-gamma treated U-937 cells was stimulated by My 43 but not by other IgM mAb recognizing myeloid cells. By these criteria My 43 recognized a molecule capable of triggering function. Moreover, its binding reactivity, ability to block binding of IgA and IgA-complexes, and its ability to induce activation of IgA receptor bearing myeloid cells, are consistent with the possibility that My 43 reacts with the IgA receptor on these cells.
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