Abstract
A panel of mutant antibodies of the phosphocholine (PC)-binding antibody, T15, was tested for binding to PC-protein, Streptococcus pneumoniae, Trichinella spiralis and Ascaris suum. Relative to wildtype T15, all the mutant antibodies showed differential recognition of the panel of PC- associated antigens. These mutant antibodies contain amino acid replacements in the CDR2 region of the heavy chain variable region, indicating the importance of CDR2 in recognition of carrier determinants. A model of T15 is shown that illustrates the strategic placement of mutations that could allow interaction with determinants associated with PC. A direct implication of this finding is that the T15 antibody combining site accommodates structures larger than phosphocholine and that recognition of associated carrier determinants could be a significant force in shaping the immune response to PC-containing pathogens.
Original language | English (US) |
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Pages (from-to) | 205-211 |
Number of pages | 7 |
Journal | Molecular Immunology |
Volume | 36 |
Issue number | 3 |
DOIs | |
State | Published - Feb 1999 |
Keywords
- Antibody CDR
- Mutation
- Phosphocholine
- T15 antibody
ASJC Scopus subject areas
- Immunology
- Molecular Biology