Suppression of MOG- and PLP-induced experimental autoimmune encephalomyelitis using a novel multivalent bifunctional peptide inhibitor
Copyright policy )Suppression of MOG- and PLP-induced experimental autoimmune encephalomyelitis using a novel multivalent bifunctional peptide inhibitor
Previously, bifunctional peptide inhibitors (BPI) with a single antigenic peptide have been shown to suppress experimental autoimmune encephalomyelitis (EAE) in an antigen-specific manner. In this study, a multivalent BPI (MVBMOG/PLP) with two antigenic peptides derived from myelin oligodendrocyte glycoprotein (MOG38-50) and myelin proteolipid protein (PLP139-151) was evaluated in suppressing MOG38-50- and PLP139-151-induced EAE. MVBMOG/PLP significantly suppressed both models of EAE even when there was some evidence of epitope spreading in the MOG38-50-induced EAE model. In addition, MVBMOG/PLP was found to be more effective than PLP-BPI and MOG-BPI in suppressing MOG38-50-induced EAE. Thus, the development of MVB molecules with broader antigenic targets can lead to suppression of epitope spreading in EAE.
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Experimental autoimmune encephalomyelitis, Encephalomyelitis, Autoimmune, Experimental, Molecular Sequence Data, T cell, Bifunctional peptide inhibitor, Epitope spreading, 540, Peptide Fragments, Mice, Inbred C57BL, Epitopes, Mice, Animals, Antigen-presenting cell, Female, Myelin-Oligodendrocyte Glycoprotein, Amino Acid Sequence, Myelin Proteolipid Protein, Peptides
Experimental autoimmune encephalomyelitis, Encephalomyelitis, Autoimmune, Experimental, Molecular Sequence Data, T cell, Bifunctional peptide inhibitor, Epitope spreading, 540, Peptide Fragments, Mice, Inbred C57BL, Epitopes, Mice, Animals, Antigen-presenting cell, Female, Myelin-Oligodendrocyte Glycoprotein, Amino Acid Sequence, Myelin Proteolipid Protein, Peptides
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