Literature DB >> 1371791

Immunoreactivity of a 10-kDa antigen of Mycobacterium tuberculosis.

P F Barnes1, V Mehra, B Rivoire, S J Fong, P J Brennan, M S Voegtline, P Minden, R A Houghten, B R Bloom, R L Modlin.   

Abstract

Identification of Ag of Mycobacterium tuberculosis recognized by T cells is essential to understanding the pathogenesis of tuberculosis and mechanism(s) of resistance to infection. Previous studies evaluating the immunoreactivity of nitrocellulose transfers of M. tuberculosis Ag separated by SDS-PAGE indicated that a high proportion of M. tuberculosis-reactive T cell lines proliferate in response to a 10-kDa Ag. We therefore purified this Ag from M. tuberculosis culture filtrates and evaluated its immunoreactivity in patients with tuberculous infection. Proliferative responses of PBMC to the 10-kDa Ag were similar to those induced by whole M. tuberculosis and greater than those elicited by other proteins isolated from culture filtrate. Furthermore, in patients with tuberculous pleuritis, proliferative responses to the 10-kDa Ag were higher in pleural fluid mononuclear cells than in PBMC, indicating that T cell reactivity to this Ag is enhanced at the site of disease. The first 15 amino acids of the 10-kDa Ag were identical to those defined previously for Bacillus Calmette-Guérin-a (BCG-a), and a T cell clone recognized the 10-kDa Ag and a peptide of BCG-a, indicating that the 10-kDa Ag corresponds to BCG-a. This Ag elicited IFN-gamma production by pleural fluid mononuclear cells and by PBMC from healthy tuberculin reactors, suggesting that the 10-kDa Ag can enhance macrophage activation and resistance to mycobacterial infection. Our findings indicate that the 10-kDa Ag of M. tuberculosis is highly immunoreactive and should be evaluated for its capacity to elicit protective immunity.

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Year:  1992        PMID: 1371791

Source DB:  PubMed          Journal:  J Immunol        ISSN: 0022-1767            Impact factor:   5.422


  25 in total

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2.  Selective T-cell recognition of the N-terminal peptide of GroES in tuberculosis.

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Journal:  Infect Immun       Date:  2002-03       Impact factor: 3.441

Review 3.  Heat shock proteins in immune reactions.

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Review 4.  Genetic vaccination against tuberculosis.

Authors:  D B Lowrie; C L Silva; R E Tascon
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5.  In vitro restoration of T cell responses in tuberculosis and augmentation of monocyte effector function against Mycobacterium tuberculosis by natural inhibitors of transforming growth factor beta.

Authors:  C S Hirsch; J J Ellner; R Blinkhorn; Z Toossi
Journal:  Proc Natl Acad Sci U S A       Date:  1997-04-15       Impact factor: 11.205

6.  Mycobacterium tuberculosis expresses two chaperonin-60 homologs.

Authors:  T H Kong; A R Coates; P D Butcher; C J Hickman; T M Shinnick
Journal:  Proc Natl Acad Sci U S A       Date:  1993-04-01       Impact factor: 11.205

7.  Fibronectin-binding antigen 85 and the 10-kilodalton GroES-related heat shock protein are the predominant TH-1 response inducers in leprosy contacts.

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Journal:  Infect Immun       Date:  1995-01       Impact factor: 3.441

8.  Leprosy patients with lepromatous disease recognize cross-reactive T cell epitopes in the Mycobacterium leprae 10-kD antigen.

Authors:  R Hussain; H M Dockrell; F Shahid; S Zafar; T J Chiang
Journal:  Clin Exp Immunol       Date:  1998-11       Impact factor: 4.330

9.  Mycobacterium tuberculosis heat shock protein 10 increases both proliferation and death in mouse P19 teratocarcinoma cells.

Authors:  G Galli; P Ghezzi; P Mascagni; F Marcucci; M Fratelli
Journal:  In Vitro Cell Dev Biol Anim       Date:  1996 Jul-Aug       Impact factor: 2.416

10.  Cytokine production at the site of disease in human tuberculosis.

Authors:  P F Barnes; S Lu; J S Abrams; E Wang; M Yamamura; R L Modlin
Journal:  Infect Immun       Date:  1993-08       Impact factor: 3.441

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