Premium
The MT4 Allodeterminant Is Borne on an HLA‐DS Molecule on DR5 Cells
Author(s) -
ZANGARA R. J.,
KANNAPELL C. C.,
KARR R. W.,
GOYERT S.,
SILVER J.,
SCHWARTZ B. D.
Publication year - 1984
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1984.tb00999.x
Subject(s) - immunoprecipitation , molecule , microbiology and biotechnology , human leukocyte antigen , chemistry , biology , stereochemistry , biochemistry , cell culture , genetics , antigen , organic chemistry
Human HLA‐DR molecules have been shown to be structurally homologous to the murine I‐E subregion molecules by amino acid sequence analysis. Recent studies have demonstrated the isolation of an I‐A subregion‐homologous molecule (HLA‐DS) from human B‐cell lines with the rabbit antiserum RbO3, made against a marmoset I‐A‐like Ia molecule. Previous work from our laboratory has demonstrated that the DR5 homozygous lymphoblastoid cell line Swei expresses at least two different Ia α chains and four different Ia β chains, which associate to form four distinct human Ia molecules, α 1 β 2 , α 1 β 3 , α 2 β 1 , and α 2 β 4 , and that the α 2 β 1 molecule bears the allodeterminants MB3 and MT4. To determine whether the MT4‐bearing α 2 β 1 molecule was an HLA‐DS molecule, the α 2 β 1 molecule reactive with an anti‐MT4 alloserum was compared with the Ia molecule reactive with the rabbit xenoantiserum RbO3 by two‐dimensional gel electrophoresis and sequential immunoprecipitation. The α 2 chain and the RbO3‐reactive α chain yielded essentially similar spot patterns. The β 1 ‐chain spot pattern was a subset of the RbO3‐reactive β‐chain spot pattern. Sequential immunoprecipitation indicated that RbO3 removed all molecules reactive with MGH88B. These results indicate that on DR5 cells the allosera‐reactive α 2 β 1 molecule, which bears MT4, is an HLA‐DS molecule.