Abstract
We have recently described an anti-β2-microglobulin (β2-m) monoclonal antibody (mAb 14H3) capable of recognizing the epitope 92-99 of the protein in the monomeric native state as well as in the fibrillar polymeric state, but not in the major histocompatibility complex type I (MHCI) anchored to the cell membrane. In the present study, we investigated the molecular basis for the inaccessibility of the C-terminal end of β2-m in the MHCI complex, and demonstrated that mAb 14H3 binds the soluble fraction of the MHCI complex with a K(d) of 0.3 μM. An interaction between the complex and the membrane protects β2-m from immunological recognition at the MHCI level. This protection from antibody recognition can be weakened by procedures such as heat shock or γ irradiation that perturb the membrane structure and commit the cell to the apoptotic pathway. mAb 14H3 can recognize MHCI in a transient state that most likely precedes β2-m shedding and may be proposed as a useful tool for dynamic analysis of MHCI conformational modifications.
Original language | English |
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Pages (from-to) | 675-683 |
Number of pages | 9 |
Journal | Cellular and Molecular Life Sciences |
Volume | 57 |
Issue number | 4 |
Publication status | Published - 2000 |
Keywords
- β-Microglobulin
- Amyloidosis
- Apoptosis
- Major histocompatibility antigen type I
- Monoclonal antibody
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
- Cell Biology