Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0019163 (hepatitis B)
 38,309 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A murine/human chimeric antibody with specificity for hepatitis B surface antigen has been produced by genetic engineering. The light and heavy chain variable region exons encoding the murine monoclonal antibody 2H1 were isolated and inserted into mammalian expression vectors containing the human kappa and gamma 1 constant region exons. The chimeric genes were transfected into murine SP2/0 hybridoma cells by electroporation, and transfectomas secreting chimeric antibody were isolated. Secretion levels ranged from 1-7pg/(cell.24hr). The chimeric antibody bound specifically to hepatitis B surface antigen and competed effectively with the parental murine monoclonal antibody for binding to these sites. Chimeric 2H1 is the first clinically relevant, genetically engineered anti-viral antibody and may represent an improved agent for the prevention of hepatitis B virus transmission.
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PMID:[Construction, expression and characterization of a murine/human chimeric antibody with specificity for hepatitis B surface antigen]. 215 88

A murine/human chimeric antibody with specificity for Hepatitis B surface antigen has been produced by genetic engineering. The light and heavy chain variable region exons encoding the murine monoclonal antibody 2H1 were isolated and inserted into mammalian expression vectors containing the human kappa and gamma 1 constant region exons. The chimeric genes were transfected into murine Sp2/0 hybridoma cells by electroporation and transfectomas secreting chimeric antibody were isolated. Secretion levels ranged from 1-7 pg/cell/24 hr. The chimeric antibody bound specifically to Hepatitis B surface antigen and competed effectively with the parental murine monoclonal antibody for binding to these sites. Chimeric 2H1 is the first clinically relevant, genetically engineered anti-viral antibody and may represent an improved agent for the prevention of hepatitis B virus transmission.
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PMID:Construction, expression and characterization of a murine/human chimeric antibody with specificity for hepatitis B surface antigen. 234 91

From a panel of monoclonal antibodies (MoAbs) directed against E. coli-derived native and denatured hepatitis B virus (HBV) core antigen we have selected a set of specific MoAbs which recognize different linear antigenic determinants: MoAb C1-5--cl epitope; MoAb 14K8--less immunogenic N-terminal region; and MoAbs 13C9, 10F10 and 14E11, 14G3--the immunodominant region between amino acids 134 and 140. We have applied the polymerase chain reaction technique to clone Ig VH and VL region genes, and appropriate full-length cDNA clones were obtained and characterized by nucleotide sequence analysis. Among the six heavy chain variable region sequences examined, three VH families were represented. Two of them belong to the 7183 (MoAb C1-5) and 3609 (14B8) families respectively and four, having only two amino acid changes in the CDR2 region, to the J558 family. These four probably are derived from a single expanded B-cell clone. The light chain sequences indicate that their VL are encoded by V kappa 21, V kappa 19 and V kappa 3 germline genes. Unlike VH genes, light chain genes are closely related to known representatives of mouse kappa light chain families and are employed also by MoAbs raised against other antigens.
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PMID:The structure of the variable regions of mouse monoclonal antibodies to hepatitis B virus core antigen. 831 61

A murine monoclonal antibody H67 was characterized for the binding specificity, which showed that H67 recognizes a disulfide-bond-dependent conformational epitope of common a antigenic determinant on the hepatitis B surface antigen. The result suggested that this antibody may have the potential of replacing hepatitis B immune globulin in the prevention of hepatitis B virus (HBV) infection. Therefore, we have constructed the humanized antibody HuS10 by grafting the complementarity determining regions and some framework amino acid residues of H67 onto the most homologous human antibody variable regions, 21/28 for heavy chain variable region and B1 and J kappa 2 for light chain variable region, followed by combining with human constant regions C gamma 1 and C kappa. The affinity of the HuS10 was the same as that of the H67, 8 x 10(8) x 10(8)M-1, and the HuS10 neutralized the in vitro infection of adult human hepatocyte primary culture by adr or ayw subtype of HBV. The neutralization assay showed that the HuS10 had approximately 2,000-times higher specific activity than commercially available polyclonal HBIG. These results suggest that the humanized antibody will be useful in the prevention or treatment of HBV infection.
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PMID:A humanized antibody with specificity for hepatitis B surface antigen. 905 59

The nucleotide sequence of the monoclonal antibody F124, specific for the preS2 region of the surface antigen of hepatitis B virus, has been determined and an single-chain Fv fragment (scFv) recombinant construction has been cloned and expressed into the periplasmic region of Escherichia coli. The recombinant antibody fragment contains a (Gly4Ser)3 linker connecting the C-terminus of the heavy chain variable region (V(L)) domain to the N-terminus of the light chain variable region (V(L)) domain. A 23-residue peptide segment, containing a c-myc marker for immunochemical detection of the scFv and hexahistidine tag to facilitate its purification, was added C-terminal to the V(L) domain. The scFv mimics the antibody in binding to the native antigen in the form of recombinant hepatitis B surface antigen (HBsAg) particles as well as to peptide fragments carrying the viral epitope.
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PMID:Sequence analysis of a monoclonal antibody specific for the preS2 region of hepatitis B surface antigen, and the cloning, expression and characterisation of its single-chain Fv construction. 989 81

We have constructed a humanized antibody with specificity for the pre-S2 surface antigen of hepatitis B virus (HBV) by grafting the complementarity determining regions (CDRs) of parental murine monoclonal antibody (mAb) into human anti-Sm antibody framework regions. The humanized antibody has a substitution at position 94 in a framework region of the heavy chain variable region, and exhibits the same antigen binding affinity as the parental murine monoclonal and chimeric antibodies. In order to assess the stability of these antibodies, thermal inactivation of the parental, chimeric and humanized antibodies was analyzed. Fifty percent inactivation of the chimeric and humanized antibodies was observed at 63.7 degrees C and 68.7 degrees C, respectively, compared to 55.0 degrees C for murine antibody. The humanized antibody also exhibited increased stability against denaturant. Guanidine-induced unfolding monitored by the changes in fluorescence intensity at 360 nm showed that midpoints of the transition of the chimeric and humanized antibodies were 2.47 M and 2.56 M, respectively, whereas that of the murine antibody was 1.36 M.
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PMID:Stability of murine, chimeric and humanized antibodies against pre-S2 surface antigen of hepatitis B virus. 1462