Amino acid residue substitution at t-cell determinant-flanking sites in β-lactoglobulin modulates antigen presentation to t cells through subtle conformational change

Akio Ametani, Toshio Sakurai, Yoshinori Katakura, Satoru Kuhara, Hideki Hirakawa, Tomohiro Hosoi, Shun Ichi Dosako, Shuichi Kaminogawa

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

We compared T-cell responses to regions in residues 21-40 of A and B variants of bovine milk β-lactoglobulin (β-LG) that vary by two different amino acid residues at 64 and 118. Results showed that T cells from C57/BL6 and C3H/HeN mice immunized with peptide 21-40 or BALB/c mice immunized with peptide 21-32 or 25-40 responded more vigorously to β-LG B than to β-LG A. This difference in response to 25-40 in BALB/c mice was not observed when β-LGs B and A were denatured, suggesting that the conformation difference affects display of the determinant 25-40. Reactivity of anti-β-LG monoclonal antibodies and molecular modeling using molecular dynamics calculations revealed subtle differences in the three-dimensional structure of these two variants. Furthermore, substitution of two amino acid residues at sites distant from the T-cell determinant induced differential determinant display on antigen-presenting cells, possibly due to subtle conformational changes in β-LG.

Original languageEnglish
Pages (from-to)1507-1514
Number of pages8
JournalBioscience, Biotechnology and Biochemistry
Volume67
Issue number7
DOIs
Publication statusPublished - Jan 1 2003

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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