Abstract
Cytotoxic T lymphocyte-associated antigen-4 (CTLA-4; CD152) is a transmembrane protein that is structurally similar to CD28. As CTLA-4 has a much higher binding affinity to B7 than CD28, several approaches using soluble CTLA-4 have been tried to down-regulate T cell activity by blocking the interaction between CD28 and B7. We constructed soluble rhesus monkey CTLA-4 immunoglobulin (CTLA-4Ig) containing a critical binding site to B7 combined with a constant Ig heavy chain region in a mammalian system. Flow cytometry analyses indicated that soluble rhesus monkey CTLA-4Ig bound to rhesus monkey CD86 (B7. 2). Moreover, soluble rhesus monkey CTLA-4Ig more effectively blocked the rhesus monkey-rhesus monkey allogeneic mixed lymphocyte reaction compared with that of humans. These results indicate that soluble rhesus monkey CTLA-4Ig may be useful in preclinical trials in a rhesus monkey model.
Original language | English |
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Pages (from-to) | 2191-2197 |
Number of pages | 7 |
Journal | Biotechnology letters |
Volume | 34 |
Issue number | 12 |
DOIs | |
Publication status | Published - 2012 Nov |
Keywords
- Allogeneic response
- Co-stimulatory molecule
- Cytotoxic T lymphocyte-associated antigen-4
- Mixed lymphocyte reaction
- Rhesus monkey
- T cells
ASJC Scopus subject areas
- Biotechnology
- Bioengineering
- Applied Microbiology and Biotechnology