Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0026918 (Mycobacterium)
 52,428 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A panel of monoclonal antibodies were derived from BALB.B10 mice immunized with a culture filtrate from Mycobacterium tuberculosis H37Rv. Of these antibodies, 10 were examined more closely for antigen specificity and interspecies reactivity. Six antibodies were used as immunosorbents for affinity purification of their corresponding antigens. Two monoclonal antibodies (HBT 2 and HBT 11) reacted with a 17-kilodalton antigen, and a competition assay showed that these antibodies are directed against the same epitope or against epitopes that are sterically very close to each other. Monoclonal antibody HBT 12 reacted with the same molecule with which a previously described 38-kilodalton reactive antibody reacted but was directed against a different epitope. Antibody HBT 10 reacted with a culture filtrate of M. tuberculosis but not of Mycobacterium bovis BCG. This latter finding was further studied by testing different preparations of M. tuberculosis H37Rv antigens and, additionally, culture filtrates of four M. tuberculosis and two BCG strains. Interspecies reactivity was assayed by immunoblotting and revealed that the majority of the monoclonal antibodies were specific to M. tuberculosis complex.
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PMID:Monoclonal antibodies produced in BALB.B10 mice define new antigenic determinants in culture filtrate preparations of Mycobacterium tuberculosis. 246 47

Only a limited number of proteins from Mycobacterium tuberculosis have so far been shown to possess species-specific epitopes as defined by monoclonal antibodies. One such protein is protein antigen b (Pab) of molecular weight 38,000, which binds the monoclonal antibodies HYT 28, HAT 2, HBT 12, HGT 3, TB 71, and TB 72. The gene encoding this protein was isolated from a lambda gt11 M. tuberculosis DNA library. The nucleotide sequence of the recombinant mycobacterial insert was determined, and an open reading frame of 374 amino acids was identified. The amino acid sequence exhibited 30% homology to a phosphate-binding protein, PstS, from Escherichia coli. The pab gene was subcloned into pBR322 in conjunction with the lacZ gene, and deletions were obtained from the 3' end. The anti-Pab monoclonal antibodies were used to probe crude protein lysates of E. coli transformed with the deletion plasmids. The monoclonal antibodies showed two reactivity patterns; one group of antibodies were dependent on the presence of the ultimate 91 amino acids of the protein, whereas another group of antibodies recognized an antigenic domain located on the middle portion of the molecule. None of the antibodies bound to the N-terminal 117-amino-acid peptide.
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PMID:Structure and mapping of antigenic domains of protein antigen b, a 38,000-molecular-weight protein of Mycobacterium tuberculosis. 254 26

Eleven strains of inbred mice were immunized with a culture filtrate of Mycobacterium tuberculosis H37Rv, and the quality of the antibody responses was determined by immunoblotting. The quantity of mycobacterial antigen used for each immunization ranged from 6 to 750 micrograms per inoculum. The culture filtrate of M. tuberculosis was separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and electrotransferred to nitrocellulose filters. Immunoblotting results were obtained with serum from the following 11 strains of immunized mice: C57BL/6J, BALB/cJ, BALB.B10, C3H.OH, A.CA/Sn, CBA/J, DBA/1J, DBA/2J, C3H/HeJ, B10.A/SgSn, and B10.D2/nSn. Mice were tested individually, and results from each mouse were compared after each immunization. It was found that sera from individual mice within the same strain differed only slightly in their immune response patterns. In contrast, major differences were seen when the reactivities of sera from different strains were compared. Hybridomas were obtained from cell fusions by using spleen cells from BALB.B10 and CBA/J mice. Twelve monoclonal antibodies were raised, which identified epitopes on molecules with different electrophoretic mobilities than those already described by other investigators. The monoclonal antibodies were characterized by immunoblotting with respect to their reactivities with culture filtrates from M. tuberculosis and six other mycobacterial species. One of the monoclonal antibodies (HBT-10) identified an epitope that was present in M. tuberculosis H37Rv but not in Mycobacterium bovis BCG.
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PMID:Antibody responses against Mycobacterium tuberculosis in 11 strains of inbred mice: novel monoclonal antibody specificities generated by fusions, using spleens from BALB.B10 and CBA/J mice. 313 66