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Human single-chain Fv intrabodies counteract in situ huntingtin aggregation in cellular models of Huntington's disease.
Lecerf, J M; Shirley, T L; Zhu, Q; Kazantsev, A; Amersdorfer, P; Housman, D E; Messer, A; Huston, J S.
Afiliación
  • Lecerf JM; IntraImmune Therapies, Inc., Lexington, MA 02215, USA.
Proc Natl Acad Sci U S A ; 98(8): 4764-9, 2001 Apr 10.
Article en En | MEDLINE | ID: mdl-11296304
This investigation was pursued to test the use of intracellular antibodies (intrabodies) as a means of blocking the pathogenesis of Huntington's disease (HD). HD is characterized by abnormally elongated polyglutamine near the N terminus of the huntingtin protein, which induces pathological protein-protein interactions and aggregate formation by huntingtin or its exon 1-containing fragments. Selection from a large human phage display library yielded a single-chain Fv (sFv) antibody specific for the 17 N-terminal residues of huntingtin, adjacent to the polyglutamine in HD exon 1. This anti-huntingtin sFv intrabody was tested in a cellular model of the disease in which huntingtin exon 1 had been fused to green fluorescent protein (GFP). Expression of expanded repeat HD-polyQ-GFP in transfected cells shows perinuclear aggregation similar to human HD pathology, which worsens with increasing polyglutamine length; the number of aggregates in these transfected cells provided a quantifiable model of HD for this study. Coexpression of anti-huntingtin sFv intrabodies with the abnormal huntingtin-GFP fusion protein dramatically reduced the number of aggregates, compared with controls lacking the intrabody. Anti-huntingtin sFv fused with a nuclear localization signal retargeted huntingtin analogues to cell nuclei, providing further evidence of the anti-huntingtin sFv specificity and of its capacity to redirect the subcellular localization of exon 1. This study suggests that intrabody-mediated modulation of abnormal neuronal proteins may contribute to the treatment of neurodegenerative diseases such as HD, Alzheimer's, Parkinson's, prion disease, and the spinocerebellar ataxias.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Región Variable de Inmunoglobulina / Proteínas Nucleares / Enfermedad de Huntington / Proteínas del Tejido Nervioso Tipo de estudio: Prognostic_studies Límite: Animals / Humans Idioma: En Revista: Proc Natl Acad Sci U S A Año: 2001 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Región Variable de Inmunoglobulina / Proteínas Nucleares / Enfermedad de Huntington / Proteínas del Tejido Nervioso Tipo de estudio: Prognostic_studies Límite: Animals / Humans Idioma: En Revista: Proc Natl Acad Sci U S A Año: 2001 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos