TY - JOUR
T1 - Monoclonal anti‐VH antibodies recognize a common VH determinant expressed on immunoglobulin heavy chains from various species
AU - Eshhar, Zelig
AU - Gigi, Orit
AU - Givol, David
AU - Ben‐Neriah, Yinon
PY - 1983
Y1 - 1983
N2 - Our previous work using rabbit antibodies to the variable region of MOPC315 myeloma heavy chain (VH) has indicated the existence of framework determinant(s) common to many murine heavy chains. Here we report the characterization of anti‐VH monoclonal antibodies (mAb) prepared in an attempt to elucidate the nature of the common VH determinant. We immunized AKR/J mice with a purified VH315 fragment and generated somatic cell hybrids by the fusion of the immune AKR/J splenocytes with the NS1 myeloma cells. Thirty‐seven common anti‐VH and 57 subgroup VHI‐specific hybridomas have been established and characterized. Whereas the anti‐subgroup mAb seemed to react with a determinant unique to the MOPC315 (mouse VHI) subgroup, all the anti‐VH mAb reacted with myeloma heavy chains of different VH subgroups, class and allotypes. Antibody competition studies revealed that the VH subgroup determinants are distinct from the common VH determinants and that both were also recognized by the rabbit polyclonal antibodies. The common VH determinants were found to be “hidden” determinants on intact immunoglobulin molecules being exposed only on isolated heavy chains. Furthermore, they are sequential determinants since they are preserved on fully denatured heavy chains. The common VH determinants are shared by immunoglobulins of a wide range of vertebrates from amphibia to man and thus represent antigenic structures which were highly conserved throughout evolution.
AB - Our previous work using rabbit antibodies to the variable region of MOPC315 myeloma heavy chain (VH) has indicated the existence of framework determinant(s) common to many murine heavy chains. Here we report the characterization of anti‐VH monoclonal antibodies (mAb) prepared in an attempt to elucidate the nature of the common VH determinant. We immunized AKR/J mice with a purified VH315 fragment and generated somatic cell hybrids by the fusion of the immune AKR/J splenocytes with the NS1 myeloma cells. Thirty‐seven common anti‐VH and 57 subgroup VHI‐specific hybridomas have been established and characterized. Whereas the anti‐subgroup mAb seemed to react with a determinant unique to the MOPC315 (mouse VHI) subgroup, all the anti‐VH mAb reacted with myeloma heavy chains of different VH subgroups, class and allotypes. Antibody competition studies revealed that the VH subgroup determinants are distinct from the common VH determinants and that both were also recognized by the rabbit polyclonal antibodies. The common VH determinants were found to be “hidden” determinants on intact immunoglobulin molecules being exposed only on isolated heavy chains. Furthermore, they are sequential determinants since they are preserved on fully denatured heavy chains. The common VH determinants are shared by immunoglobulins of a wide range of vertebrates from amphibia to man and thus represent antigenic structures which were highly conserved throughout evolution.
UR - http://www.scopus.com/inward/record.url?scp=0020788446&partnerID=8YFLogxK
U2 - 10.1002/eji.1830130704
DO - 10.1002/eji.1830130704
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C2 - 6191996
AN - SCOPUS:0020788446
SN - 0014-2980
VL - 13
SP - 533
EP - 540
JO - European Journal of Immunology
JF - European Journal of Immunology
IS - 7
ER -