lipid-a and Cell-Transformation--Viral

lipid-a has been researched along with Cell-Transformation--Viral* in 2 studies

Other Studies

2 other study(ies) available for lipid-a and Cell-Transformation--Viral

Article	Year
Human--human hybridomas secreting lipid A reactive monoclonal antibodies. Immunology letters, 1988, Volume: 18, Issue:2 Five human-human hybridoma cell lines secreting monoclonal antibodies (mAbs) against lipid A (LA) were produced by cell fusion of Epstein-Barr virus (EBV) transformed human peripheral blood lymphocytes and a human lymphoblastoid cell line KR-4. All these mAbs were isotyped as IgM(kappa) and reacted with lipopolysaccharides (LPS) and LA of various gram-negative bacteria. Whereas the binding of only four of the five mAbs to solid-phase LA was blocked by polymyxin-B sulphate, the mitogenic effect of LPS and LA on murine B lymphocytes was inhibited by all five mAbs. These results demonstrate that the human immune system recognizes at least two common epitopes in lipid A of various gram-negative bacteria. Topics: Antibodies, Monoclonal; Antigens, Bacterial; Cell Transformation, Viral; Epitopes; Herpesvirus 4, Human; Humans; Hybridomas; In Vitro Techniques; Lipid A	1988
Human monoclonal antibodies that recognize conserved epitopes in the core-lipid A region of lipopolysaccharides. The Journal of clinical investigation, 1987, Volume: 79, Issue:5 Epstein-Barr virus (EBV)-transformed human B lymphocytes were fused with a murine-human heteromyeloma to produce stable hybrid cell lines that secreted human monoclonal antibodies (mAbs) of the IgM class that recognized conserved epitopes in the core-lipid A region of lipopolysaccharides (LPS). Three of the mAbs reacted with epitopes on the lipid A moiety, while a fourth recognized a determinant in the core oligosaccharide. The lipid A-specific mAbs cross-reacted with heterologous rough LPS and with lipid As released by acid hydrolysis of different intact (smooth) LPS. Carbohydrate groups in the O-side chain and core oligosaccharide of isolated, smooth LPS restricted antibody access to antigenic sites on lipid A. Yet, one lipid A-reactive mAb recognized its epitope on the surfaces of a variety of intact bacteria. These findings confirm the presence of highly conserved epitopes in the core-lipid A complex and prove the existence of human B cell clones with the potential for secreting high avidity IgM antibodies that react with these widely shared determinants. Such human mAbs might provide protective activity against disease caused by diverse gram-negative bacteria. Topics: Animals; Antibodies, Monoclonal; Antibody Specificity; B-Lymphocytes; Cell Transformation, Viral; Cross Reactions; Enzyme-Linked Immunosorbent Assay; Epitopes; Gram-Negative Bacteria; Herpesvirus 4, Human; Humans; Lipid A; Lipopolysaccharides; Mice	1987

Article

Year

Human--human hybridomas secreting lipid A reactive monoclonal antibodies.

Immunology letters, 1988, Volume: 18, Issue:2

Five human-human hybridoma cell lines secreting monoclonal antibodies (mAbs) against lipid A (LA) were produced by cell fusion of Epstein-Barr virus (EBV) transformed human peripheral blood lymphocytes and a human lymphoblastoid cell line KR-4. All these mAbs were isotyped as IgM(kappa) and reacted with lipopolysaccharides (LPS) and LA of various gram-negative bacteria. Whereas the binding of only four of the five mAbs to solid-phase LA was blocked by polymyxin-B sulphate, the mitogenic effect of LPS and LA on murine B lymphocytes was inhibited by all five mAbs. These results demonstrate that the human immune system recognizes at least two common epitopes in lipid A of various gram-negative bacteria.

Topics: Antibodies, Monoclonal; Antigens, Bacterial; Cell Transformation, Viral; Epitopes; Herpesvirus 4, Human; Humans; Hybridomas; In Vitro Techniques; Lipid A

1988

Human monoclonal antibodies that recognize conserved epitopes in the core-lipid A region of lipopolysaccharides.

The Journal of clinical investigation, 1987, Volume: 79, Issue:5

Epstein-Barr virus (EBV)-transformed human B lymphocytes were fused with a murine-human heteromyeloma to produce stable hybrid cell lines that secreted human monoclonal antibodies (mAbs) of the IgM class that recognized conserved epitopes in the core-lipid A region of lipopolysaccharides (LPS). Three of the mAbs reacted with epitopes on the lipid A moiety, while a fourth recognized a determinant in the core oligosaccharide. The lipid A-specific mAbs cross-reacted with heterologous rough LPS and with lipid As released by acid hydrolysis of different intact (smooth) LPS. Carbohydrate groups in the O-side chain and core oligosaccharide of isolated, smooth LPS restricted antibody access to antigenic sites on lipid A. Yet, one lipid A-reactive mAb recognized its epitope on the surfaces of a variety of intact bacteria. These findings confirm the presence of highly conserved epitopes in the core-lipid A complex and prove the existence of human B cell clones with the potential for secreting high avidity IgM antibodies that react with these widely shared determinants. Such human mAbs might provide protective activity against disease caused by diverse gram-negative bacteria.

Topics: Animals; Antibodies, Monoclonal; Antibody Specificity; B-Lymphocytes; Cell Transformation, Viral; Cross Reactions; Enzyme-Linked Immunosorbent Assay; Epitopes; Gram-Negative Bacteria; Herpesvirus 4, Human; Humans; Lipid A; Lipopolysaccharides; Mice

1987