T-cell Recognition and Antigen Presentation of Myoglobin. Protein Recognition by Site-specific T-cell Clones is Influenced by Amino Acid Substitutions Outside the Site

Overview

Journal Biochem J

Specialty Biochemistry

Date 1989 Mar 15

PMID 2786412

Citations 2

Authors

M Yoshioka

M Z Atassi

Affiliations

Soon will be listed here.

Abstract

Six T-cell clones from SJL mice were prepared from T-cell lines that were obtained by passage with synthetic myoglobin (Mb) peptide 107-120. In addition, a T-cell clone, specific to this region of Mb, was isolated from a Mb-passaged T-cell culture. The proliferative responses of these clones to Mb variants from 14 different species were studied. It was found, as expected, that amino acid replacements within the site affected its recognition by the T-cell clones. In addition to these effects, the T-cell recognition site, like the sites recognized by antibodies, was also influenced by substitutions of residues that are close to site residues in three-dimensional structure but are otherwise distant in sequence. This is noteworthy in view of the fact that six of the clones were selected with a free peptide, and thus the environmental residues are clearly not part of the 'contact' residues of the site. These findings are discussed in relation to the presentation of the antigen and are interpreted as indicating that Mb is presented in its intact form to the T-cells in vitro.

Citing Articles

T cells specific for alpha-beta interface regions of hemoglobin recognize the isolated subunit but not the tetramer and indicate presentation without processing.

Atassi M, Yoshioka M, Bixler Jr G Proc Natl Acad Sci U S A. 1989; 86(17):6729-33.

PMID: 2788890 PMC: 297919. DOI: 10.1073/pnas.86.17.6729.

Conformation-dependent recognition of a protein by T cells requires presentation without processing.

Atassi M, Bixler Jr G, Yokoi T Biochem J. 1989; 259(3):731-5.

PMID: 2471511 PMC: 1138579. DOI: 10.1042/bj2590731.

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