Profiles of skin test reactivity to antigens of various mycobacterial species in a human population and in experimental infections

Vandiviere, H. M.; Melvin, Irene G.; Narain, Ravin; Harris, W.D.M.; Chaparas, Sotiros D.

doi:10.1016/0041-3879(80)90045-8

Tubercle

1980

DOI: 10.1016/0041-3879(80)90045-8

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Profiles of skin test reactivity to antigens of various mycobacterial species in a human population and in experimental infections

H. M. Vandiviere

Irene G. Melvin

Ravin Narain

et al.

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Cited by 7 publications

(1 citation statement)

References 27 publications

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“…The antigenic cross-reactivity of purified protein derivatives is a major problem for disease diagnosis. Improvement of immunodiagnostic screening for M. bovis and M. tuberculosis infection therefore relies on the identification and purification of antigens exhibiting a high degree of specificity (4,39,40). To date a number of promising candidate antigens have been identified (8,46).…”

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confidence: 99%

Secretion of the mycobacterial 19-kilodalton protein by Escherichia coli, a novel method for the purification of recombinant mycobacterial antigens

Hewinson

Harris

Whelan

et al. 1996

Clin Diagn Lab Immunol

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the secretion by Escherichia coli of a recombinant form of the immunogenic protein MPB70 of Mycobacterium bovis when the protein is translated from its native initiation codon. N-terminal sequence analysis of the purified protein revealed that the signal peptide of MPB70 was cleaved by an endopeptidase of E. coli at the same cleavage site as reported for the protein in M. bovis. Since both the Band T-cell antigenicities of the purified recombinant protein were similar to that of the native protein, the 19-kDa antigen of M. bovis was used as a model to test whether the signal peptide of MPB70 could direct the secretion of heterologous proteins in E. coli and whether antigen produced in this way retained antigenicity superior to that of recombinant protein produced as a fusion to glutathione-S-transferase. A chimeric protein was produced in which the signal peptide of MPB70 was fused to the 19-kDa antigen of M. bovis at amino acid residue 23. This chimeric protein was found to be secreted into the periplasm and culture medium of recombinant E. coli, and the signal peptide was cleaved by an endopeptidase of E. coli during secretion. Secretion of the 19-kDa antigen facilitated purification of the antigen by two-stage preparative electrophoresis which gave yields of 2.5 mg of purified, soluble 19-kDa antigen from 2.5 g (wet weight) of E. coli. Antigen purified in this way retained both Band T-cell antigenicities. Moreover, the nonspecific mitogenic activity of the purified 19-kDa antigen was low, while the magnitude of the T-cell response induced by the purified antigen was considerably higher than that observed with purified antigen produced as a fusion protein with glutathione-S-transferase.

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mentioning

confidence: 99%

Secretion of the mycobacterial 19-kilodalton protein by Escherichia coli, a novel method for the purification of recombinant mycobacterial antigens

Hewinson

Harris

Whelan

et al. 1996

Clin Diagn Lab Immunol

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show abstract

Sensitivity to sensitins and tuberculin in Swedish children II. A study of preschool children

et al. 1991

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Skin testing with recombinant Mycobacterium intracellulare antigens

Morris

Mackall

Malik

et al. 1992

Tubercle and Lung Disease

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Profiles of skin test reactivity to antigens of various mycobacterial species in a human population and in experimental infections

Cited by 7 publications

References 27 publications

Secretion of the mycobacterial 19-kilodalton protein by Escherichia coli, a novel method for the purification of recombinant mycobacterial antigens

Secretion of the mycobacterial 19-kilodalton protein by Escherichia coli, a novel method for the purification of recombinant mycobacterial antigens

Sensitivity to sensitins and tuberculin in Swedish children II. A study of preschool children

Skin testing with recombinant Mycobacterium intracellulare antigens

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