Use of Anti‐(β2 Microglobulin) mAb to Study Formation of Amyloid Fibrils
- 1 October 1997
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 249 (1), 21-26
- https://doi.org/10.1111/j.1432-1033.1997.t01-2-00021.x
Abstract
Three mAbs, IgG1k 1F11, 7B6 and 14H3, were raised against in vitro-self-aggregated beta2-microglobulin. They recognize the native and unfolded forms of the protein and bind its fibrillar form that is present in amyloid tissue. When assayed in fibrillogenesis tests in vitro, mAb 14H3 inhibited fibril formation from beta2-microglobulin. This mAb recognizes a sequential epitope corresponding to the C-terminal octapeptide, residues 92-99, of beta2-microglobulin. By using synthetic peptides it has been found that the integrity of the sequence is essential for the formation of the immunocomplex: the binding affinity is lowered by one order of magnitude (Kd from 10(-7) M to 10(-6) M) by removal of Met99 and completely abolished when both Asp98 and Met99 are lost or Arg98 is substituted with Lys. The other two mAbs, 1F11 and 7B6, which bind sequences 20-41 and 63-75, respectively, are without effect on beta2-microglobulin fibrillogenesis. These two mAbs recognize beta2-microglobulin bound to the heavy chain in the major histocompatibility complex of type I located in the cell membrane, a property which is not shared by mAb 14H3.Keywords
This publication has 18 references indexed in Scilit:
- Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesisNature, 1997
- Arrest of -Amyloid Fibril Formation by a Pentapeptide LigandJournal of Biological Chemistry, 1996
- Beta 2 microglobulin isoforms in healthy individuals and in amyloid depositsKidney International, 1995
- Characterization of the Two Unique Human Anti-Flavin Monoclonal ImmunoglobulinsEuropean Journal of Biochemistry, 1995
- β‐Cyclodextrin interacts with the Alzheimer amyloid β‐A4 peptideFEBS Letters, 1994
- Use of an Anti‐Idiotypic Monoclonal Antibody in Studying Amyloidogenic Light Chains in Cells, Urine and Fibrils: Pathophysiology and Clinical ImplicationsScandinavian Journal of Immunology, 1992
- Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolutionJournal of Molecular Biology, 1991
- Normal transthyretin and synthetic transthyretin fragments from amyloid-like fibrils in vitroBiochemical and Biophysical Research Communications, 1991
- In vitro formation of amyloid fibrils from intact β2-microglobulinBiochemical and Biophysical Research Communications, 1985
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970