2 research outputs found
IgE and IgG epitope mapping by microarray peptideimmunoassay reveals the importance and diversity of the immune response to the IgG3 equine immunoglobulin
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Previous issue date: 2014Funda莽茫o Oswaldo Cruz. Instituto Nacional de Ci锚ncia e Tecnologia de Inova莽茫o em Doen莽as Negligenciadas (INCT-IDN). Centro de Desenvolvimento Tecnol贸gico em Sa煤de. Rio de Janeiro, RJ, Brasil /Universidade Federal Fluminense. Departamento de Biologia Celular e Molecular. Niter贸i, RJ, Brasil.Universidade Federal Fluminense. Departamento de Biologia Celular e Molecular. Niter贸i, RJ, Brasil.Universidade Federal Fluminense. Departamento de Biologia Celular e Molecular. Niter贸i, RJ, Brasil.Instituto Vital Brasil. Laborat贸rio de Pesquisa e Desenvolvimento. Niter贸i, RJ, Brasil.Instituto Vital Brasil. Laborat贸rio de Pesquisa e Desenvolvimento. Niter贸i, RJ, Brasil.Funda莽茫o Oswaldo Cruz. Instituto Nacional de Ci锚ncia e Tecnologia de Inova莽茫o em Doen莽as Negligenciadas (INCT-IDN). Rio de Janeiro, RJ, Brasil.The presence of whole horse IgG in therapeutic snake antivenom preparations of high
purity is a contamination that can cause IgE-mediated allergic reactions in patients. In this
study, the immunodominant IgE and IgG-binding epitopes in horse heavy chain IgG3 were
mapped using arrays of overlapping peptides synthesized directly onto activated cellulose
membranes. Pooled human sera from patients with and without horse antivenom allergies
were used to probe the membrane. We have demonstrated that, for both cases, individuals
produce antibodies to epitopes of sequential amino acids of horse heavy chain IgG3,
although the signal strength and specificity appear to be distinct between the two groups
of patients. A single region was found to contain the dominant allergic IgE epitope. The
critical residues involved in the binding of human IgE to the epitope were determined to
include four hydrophobic amino acids followed by polar and charged residues that formed
a coil structure. This is the first study to describe the specific amino acid sequences
involved with the immune recognition of human IgG and IgE to horse antivenom