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Titolo:
The N-terminal flanking region of the invariant chain peptide augments theimmunogenicity of a cryptic "self" epitope from a tumor-associated antigen
Autore:
Hess, AD; Thoburn, C; Chen, WR; Miura, Y; Van der Wall, E;
Indirizzi:
Johns Hopkins Univ, Dept Oncol, Div Immunol & Hematopoiesis, Baltimore, MD21231 USA Johns Hopkins Univ Baltimore MD USA 21231 poiesis, Baltimore, MD21231 USA
Titolo Testata:
CLINICAL IMMUNOLOGY
fascicolo: 1, volume: 101, anno: 2001,
pagine: 67 - 76
SICI:
1521-6616(200110)101:1<67:TNFROT>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
VERSUS-HOST DISEASE; MHC CLASS-II; T-CELL RECOGNITION; CANCER; LYMPHOCYTES; SPECIFICITY; HER-2/NEU; IMMUNITY; IDENTIFICATION; IMMUNIZATION;
Keywords:
tumor vaccine; invariant chain peptide; modified Her-2/neu peptide;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Hess, AD Johns Hopkins Univ, Dept Oncol, Div Immunol & Hematopoiesis, Bunting & Blaustein Canc Res Bldg,1650 Orleans St, Baltimore, MD 21231 USA Johns Hopkins Univ Bunting & Blaustein Canc Res Bldg,1650 Orleans St Baltimore MD USA 21231
Citazione:
A.D. Hess et al., "The N-terminal flanking region of the invariant chain peptide augments theimmunogenicity of a cryptic "self" epitope from a tumor-associated antigen", CLIN IMMUNO, 101(1), 2001, pp. 67-76

Abstract

The N-terminal flanking region of the invariant chain peptide termed CLIP appears to have superagonistic properties interacting with the T cell receptor and the MHC class II molecule at or near the binding site for the bacterial superantigen Staphylococcal enterotoxin B (SEB). The present studies explored the hypothesis that the N-terminal segment of CLIP can augment the immunogenicity of cryptic "self" tumor-associated antigens. A chimeric construct of an MC class II binding peptide from the c-erb oncogene (Her-2/neu)containing the N-terminal flanking region of CLIP elicited potent antitumor activity against a Her-2/neu-positive tumor in a rat model system. Comparatively, the unmodified parent peptide was ineffective. The induction of effective antitumor immunity, however, required presentation of the chimeric peptide construct on irradiated tumor cells or the peptide construct in concert with a Her-2/neu MHC class I-restricted peptide from Her-2/neu. As revealed by adoptive transfer studies, effective protective antitumor immunityin this setting required the CD4 T helper subset. Additionally, in vitro analysis revealed that immunization with the parent peptide resulted in a weak immune response to the unmodified peptide consisting of both type 1 (IL-2, IFN-gamma) and type 2 (IL-4, IL-10) cytokine-producing cells analyzed byRT-PCR (qualitative and quantitative) and by limiting dilution assay. Comparatively, immunization with the chimeric construct elicited a potent immune response to the parent peptide with predominantly type 1 cytokine-producing cells. Taken together, the results suggest that immunization with the chimeric Her-2/neu peptide induced protective antitumor immunity. Associated with this immunization strategy was the enhancement of a type 1 cytokine response. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 10:17:59