IFN-γis a potent inducer of Ig secretion by sort-purified murine B cella activated through the mlg, but not the CD40,signaling pathway

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Abstract
To study the influence of the quaternary structure of the outer membrane protein PhoE of Escherlchla coli on the resentation of an inserted T cell epttope, an epttope comprising amino acid residues 72–85 of myeiin basic protein (MBP) was inserted at dmerent shes in PhoE. This quence is the crtticai T cell epitope in experimental autoimmune encephalomyelttis (EAE) in Lewis rats. The antigenicity and immunogenicity of two dtfferent conformational forms of the chimeric PhoE constructs, i.e. the denatured monomeric form and the native Mmeric form, were studied. tt appeared that the monomeric form, but not the natlve trimeric form of such PhoE constructs induced proitferation of the MBP7245spectfic T cell line Zla. This conformational discrepancy was independent of the site in PhoE in which the epitope was inserted. lmmunlzation with the monomeric form of PhoE constructs resutted in the priming of MBW2-85-spectfic T cells. in contrast, the Mmeric form of these constructs was much less efficient in priming such cells. differences between the monomeric and trimeric forms were most apparent when induction of EAE was studied. The monomeric form was encephalitogenic whlle the trimeric form was not Furthermore, the antigen fine spectficity, Vg usage .and encephalttogenicity of T cells triggered by immunization with a monomeric PhoE construct appead to be the same as those of T cell line Zla, which was obtained after immunization with MBP, indicating that similar cells are triggered by immunization with the epitope ether inserted in PhoE or in its native context.

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