A genetic control of humoral immune response in pigs against hen egg-white lysozyme was shown to be linked to the major histocompatibility complexSLA. This control was detected when high antigen doses were used for immunization. It was more prominent with small immunizing doses of lysozyme. Under these latter conditions,SL- A heterozygous individuals exhibited a higher response than correspondingSL- A homozygous animals, suggesting a complementation phenomenon between several genes, at least one of which is linked to the porcine MHC,SL- A.
Using antisera made against porcine S‐sulfonated heavy chains two subclasses of porcine IgG could be distinguished on the basis of antigenic determinants located on the Fc fragment. The antisera prepared against the porcine gamma chains reacted with other mammalian IgG proteins, but not with avian, amphibian or fish immunoglobulins. Antigenic determinants responsible for cross‐reactivity are further localized on the Fc′ fragment of the porcine IgG molecule. Comparable antisera, specific for porcine light chains, did not cross‐react with IgG from any of the other species tested. Porcine IgG and F(ab′)2 fragment reacted with both the anti‐heavy and anti‐light chain sera, while the Fab fragment reacted only with the anti‐light chain sera. Important antigenic determinants are thus located on the light chains and the Fc portion of the heavy chain of the porcine IgG molecule.
A genomic cosmid library constructed from DNA from a genotyped individual (JF = HLA-A11, Cw-, B38/A26, Cw7, B51) was screened for clones containing class I histocompatibility genes. Among these clones, one was found to carry a 4.8 kb Hind III fragment which is highly correlated with HLA-A11. This clone was used to transfect LMTK+ cultured mouse fibroblast transformants expressing human beta-2 microglobulin. The human beta-2 microglobulin heavy chain-associated determinant was positively detected by the M18 monoclonal antibody. HLA-A11 expression on these doubly transformed cells was specifically demonstrated by complement-dependent cytotoxicity with HLA-A11 + A3-specific but not with HLA-A3-specific monoclonal antibodies. Absorption studies with human alloantisera confirmed the presence on these cells of HLA-A11 determinants and of cross-reacting determinants which absorbed anti-HLA-A1 and -A3 alloantisera. The JF5-J27 transfected cell expressed both heavy and light chains of human class I histocompatibility genes.
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