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A unique tumor antigen produced by a single amino acid substitution

Identifieur interne : 002B24 ( Main/Exploration ); précédent : 002B23; suivant : 002B25

A unique tumor antigen produced by a single amino acid substitution

Auteurs : Paul A. Monach [États-Unis] ; Stephen C. Meredith [États-Unis] ; Christopher T. Siegel [États-Unis] ; Hans Schreiber [États-Unis]

Source :

RBID : ISTEX:9102E8296D3E74AB60AC334F7E1C2F04827972F9

English descriptors

Abstract

Abstract: Mice immunized against a cancer recognize antigens unique to that cancer, but the molecular structures of such antigens are unknown. We Isolated CD4+ T cell clones recognizing an antigen uniquely expressed on the UV-induced tumor 6132A; some clones inhibited the growth of tumors bearing the specific antigen. A T cell hybridoma was used to purify this antigen from nuclear extracts by RP-HPLC and SDS-PAGE using T cell immunoblot assays. A partial amino acid sequence was nearly identical to a sequence in ribosomal protein L9. The cDNA sequence of L9 from 6132A PRO cells differed from the normal sequence at one nucleotide; this mutation encoded histidine instead of leucine at position 47. A synthetic peptide containing this mutation was over 1000-fold more stimulatory of T cells than was the wild-type peptide. These results indicate that this unique tumor antigen is derived from a single amino acid substitution in a cellular protein.

Url:
DOI: 10.1016/1074-7613(95)90078-0


Affiliations:


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Le document en format XML

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<div type="abstract" xml:lang="en">Abstract: Mice immunized against a cancer recognize antigens unique to that cancer, but the molecular structures of such antigens are unknown. We Isolated CD4+ T cell clones recognizing an antigen uniquely expressed on the UV-induced tumor 6132A; some clones inhibited the growth of tumors bearing the specific antigen. A T cell hybridoma was used to purify this antigen from nuclear extracts by RP-HPLC and SDS-PAGE using T cell immunoblot assays. A partial amino acid sequence was nearly identical to a sequence in ribosomal protein L9. The cDNA sequence of L9 from 6132A PRO cells differed from the normal sequence at one nucleotide; this mutation encoded histidine instead of leucine at position 47. A synthetic peptide containing this mutation was over 1000-fold more stimulatory of T cells than was the wild-type peptide. These results indicate that this unique tumor antigen is derived from a single amino acid substitution in a cellular protein.</div>
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