Protective effect of a synapsin peptide genetically fused to the B subunit of Escherichia coli heat labile toxin in a rat model of autoimmune encephalomyelitis

SCERBO MJ, RUPIL LL, BIBOLINI MJ, ROTH GA, MONFERRAN CG

Wiley InterScience

Año: 2009 vol. 87 p. 2273 - 2273

span lang="en" style="FONT-SIZE: 11pt; FONT-FAMILY: Arial; mso-fareast-font-family: "Times New Roman"; mso-ansi-language: EN-US; mso-fareast-language: ES; mso-bidi-language: AR-SA">Experimental autoimmune encephalomyelitis (EAE) is an inflammatory demyelinating disease with similarities to multiple sclerosis (MS) that requires the activation of auto reactive T cells that infiltrate the central nervous system (SNC). In previous studies we have shown that intraperitoneal administration of synaptosomal antigens could suppress EAE. Herein we examined the effect in this animal model of a fusion protein comprising the C domain of synapsin Ia and the B subunit of Escherichia coli heat-labile enterotoxin (LTBSC). Oral administration to rats of low amount of LTBSC induced immunological systemic tolerance to the encephalitogenic myelin basic protein. Treatment with LTBSC prior to EAE induction diminished disease incidence, DTH reaction to mye