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F Koning

Publications and source records attributed to F Koning.

112 records · Page 7Linked to original sources

A monoclonal antibody detecting an HLA-DQwl-related determinant.

A complement fixing monoclonal antibody (moab) was prepared which reacts with a polymorphic determinant on HLA class II molecules. The moab IIB3 recognises all DQwl (DC1, MB1, LB-E12) positive cells as well as some DR4, DR7, DRw8 and DRw9 positive cells. The moab reacts mainly with B-cells and not or with only a minority of the monocytes. Segregation of the determinant with HLA-DR could be shown. The determinant is strongly expressed on DR2, DR4 and DRw6 positive cell lines but only weakly on DR1 lines. In contrast to a monoclonal antibody against a monomorphic determinant on class II molecules IIB3 did not give a distinct inhibition of the MLC nor did it inhibit the generation of CTLs in MLC as has been described for the DQwl like moab BT 3/4 (Corte et al. 1982). Immunoprecipitation indicates that IIB3 reacts with DQ-like molecules.

Antibodies, Monoclonal↗

Ia molecular localization of the DRw52 allodeterminant and the DRw52-like determinants defined by monoclonal antibodies.

DRw52 (formerly MT2) is a human Ia alloantigen that is expressed in linkage disequilibrium with DR3, 5, w6, and w8. Although there is general agreement that the DRw52 determinant resides on biochemically defined DR molecules, conflicting evidence exists regarding whether DRw52 resides on one or both DR molecules, DQ and DR molecules, or DR and BR molecules. Six anti-DRw52 allosera and three DRw52-like monoclonal antibodies were used to identify the Ia molecules that bear the DRw52 and DRw52-like determinants from DR5 and DRw6 homozygous cells. Based on these two-dimensional gel studies, the DRw52 allodeterminant appears to reside on a subset of DR molecules from DR5 and DRw6 cells. In contrast, the determinants defined by the three anti-DRw52-like monoclonal antibodies were found to reside on one DR molecule, on the second DR molecule, or on both DR molecules, respectively. Therefore, there is considerable complexity of Ia antigenic determinants that are associated with DR3, 5, w6, and w8 at the population level.

Antibodies, Monoclonal↗

A mouse monoclonal antibody detecting a DR-related MT2-like specificity: serology and biochemistry.

A mouse monoclonal antibody (7.3.19.1) was produced which reacts with class II molecules on B cells and monocytes of DR3, DR5, and/or DRw6 positive donors only. Using this moab and two others, three different groups of class II molecules could be identified. Furthermore, a differential precipitation pattern was found which correlates with a DR-related variable expression of the MT2-like polymorphic determinants on the cell surface. Addition of 7.3.19.1 to MLCs did not result in significant inhibition in controls to the two other moabs tested. Normal CTL activity was found in such a stimulated responder population.

Animals↗

Ultrastructural localization of HLA-DR and HLA-DQ molecules in Langerhans cells and B cells: an immunoelectronmicroscopic study.

Using the immunoelectronmicroscopic techniques of Lowicryl embedding and ultracryomicrotomy, the intracellular distribution of HLA class II molecules was investigated on a human B cell line and on human Langerhans cells. These techniques enabled us to localize the HLA class II molecules on fixed specimens in which mobilization or clustering induced by cross linkage with antibodies is ruled out. Compared with Lowicryl embedding, the ultracryomicrotomy clearly showed more labeling. Both in B cells and Langerhans cells, the HLA-DR molecules were predominantly found in intracellular vesicular structures and on the plasma membrane. The HLA-DQ molecules were less abundant than HLA-DR molecules in the B cells and Langerhans cells. In the B cells, HLA-DQ molecules were found on the plasma membrane and in the cytoplasm. In the Langerhans cells, some HLA-DQ molecules were also found in intracellular vesicular structures. These experiments show a different localization of HLA-DR and -DQ antigens both in Langerhans cells and B cells, suggesting a different function for these molecules. The localization of HLA-DR molecules may indicate that these molecules take part in the recycling process of the plasma membrane in B cells and Langerhans cells. The HLA-DQ molecules are not internalized or recycled by the B cells, and a limited internalization of these molecules takes place in Langerhans cells. Finally, no HLA class II or clathrin molecules were found on the Birbeck granules, suggesting that, when no cross-linking with antibodies takes place, Birbeck granules, suggesting that, when no cross-linking with antibodies takes place, Birbeck granules do not play a role in recycling of HLA class II molecules in Langerhans cells.

Antibodies, Monoclonal↗