Effect of Zinc Deficiency on the Appearance of Two Immunodominant Protein Antigens (32 kDa and 65 kDa) in Culture Filtrates of Mycobacteria

Bruyn, Jacqueline De; Bosmans, Romain; Nyabenda, J; Vooren, J. P. Van

doi:10.1099/00221287-135-1-79

Cited by 26 publications

(26 citation statements)

References 16 publications

(14 reference statements)

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“…The differential expression of the Mtb 65 kDa protein, as detected by HB28 mAb, may be related to the different nutritional environments or to the different levels of metabolic products generated during culture. De Bruyn et al reported that Sauton's medium deficient in zinc enhanced the appearance of two immunodominant protein antigens, 32 kDa and 65 kDa, in culture filtrates of several mycobacterial species (2). However in the present study, where zinc levels were not controlled, only Mtb demonstrated enhanced expression of the 65 kDa protein, not M. bovis BCG or other related mycobacterial species.…”

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confidence: 78%

Differential Expression of a Mycobacterium tuberculosis Protein Recognized by a Mouse Monoclonal Antibody

Cummings¹,

Rowland²,

Hooper³

et al. 1996

Microbiology and Immunology

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Murine monoclonal antibodies were produced against Mycobacterium tuberculosis (Mtb) using standard hybridoma procedures. By a whole cell enzyme-linked immunosorbent assay (ELISA), one monoclonal antibody (mAb), HB28, demonstrated high level specific reactivity to Mtb. Western blot analysis demonstrated reactivity to a single 65 kDa Mtb protein in the cell wall extract and culture filtrate. HB28 mAb appears to be recognizing a 65 kDa Mtb protein that is over-expressed by Mtb but not other species under certain culture conditions. Differential expression and detection of this protein by HB28 mAb may have potential for diagnostic applications.

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contrasting

confidence: 78%

Differential Expression of a Mycobacterium tuberculosis Protein Recognized by a Mouse Monoclonal Antibody

Cummings¹,

Rowland²,

Hooper³

et al. 1996

Microbiology and Immunology

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“…An increase in IgG antibody levels directed against antituberculin, anti-hsp65 or anti-P64 responses was observed in the same subgroup of patients. This was expected, since P64 fragments are present in large amounts in tuberculin [30].…”

Section: Discussionmentioning

confidence: 74%

Humoral response against heat shock proteins and other mycobacterial antigens after intravesical treatment with bacille Calmette–Guérin (BCG) in patients with superficial bladder cancer

Zlotta

Drowart

Huygen

et al. 1997

Clinical and Experimental Immunology

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SUMMARYFew studies have analysed the antibody response during intravesical BCG immunotherapy for superficial bladder cancer. We have examined the evolution in serum antibody response against several heat shock proteins (hsp), including the recombinant mycobacterial hsp65 and the native protein P64 from BCG, GroEL from Escherichia coli (hsp60 family), recombinant mycobacterial hsp70 and the E. coli DnaK (hsp70 family), against purified protein derivative of tuberculin (PPD) and the AG85 complex of Mycobacterium bovis BCG, as well as against tetanus toxoid in 42 patients with a superficial bladder tumour, 28 treated with six intravesical BCG instillations and 14 patients used as controls. We also analysed the lymphoproliferative response of peripheral blood mononuclear cells against PPD in this population. Data of antibody responses at 6 weeks post BCG were available in all 28 patients,

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“…These proteins are associated with the bacterial surface (22) and are major secretory products in Mycobacterium tuberculosis and M. bovis BCG culture fluids (1,6,12). In addition, the 30-kDa protein of this complex, referred to as antigen 85B, has been found to be among the most abundant proteins produced intracellularly in human mononuclear phagocytes (18) and has been demonstrated to be immunoprotective in a guinea pig model of pulmonary tuberculosis (15).…”

Section: Resultsmentioning

confidence: 99%

Identification of Mycobacterial Surface Proteins Released into Subcellular Compartments of Infected Macrophages

2000

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Considerable effort has focused on the identification of proteins secreted from Mycobacterium spp. that contribute to the development of protective immunity. Little is known, however, about the release of mycobacterial proteins from the bacterial phagosome and the potential role of these molecules in chronically infected macrophages. In the present study, the release of mycobacterial surface proteins from the bacterial phagosome into subcellular compartments of infected macrophages was analyzed. Mycobacterium bovis BCG was surface labeled with fluorescein-tagged succinimidyl ester, an amine-reactive probe. The fluorescein tag was then used as a marker for the release of bacterial proteins in infected macrophages. Fractionation studies revealed bacterial proteins within subcellular compartments distinct from mycobacteria and mycobacterial phagosomes. To identify these proteins, subcellular fractions free of bacteria were probed with mycobacteriumspecific antibodies. The fibronectin attachment protein and proteins of the antigen 85-kDa complex were identified among the mycobacterial proteins released from the bacterial phagosome.Mycobacterium spp. are the causative agents of a spectrum of diseases. The success of these pathogens lies in their ability to effectively exploit mononuclear phagocytes, where they invade, replicate, and persist within their mammalian hosts. Within these professional antigen-presenting cells, mycobacteria prevent the normal maturation of their phagosome and remain sequestered from the degradative compartments of the endosome/lysosome continuum (2,4,11,28,35). The mycobacterial phagosome is nonfusigenic with lysosomes (2, 4, 11, 28, 35) and fails to acidify due to lack of accumulation of proton ATPase complexes (30). This is a deviation from the normal maturation process, in which phagosomes of macrophages differentiate into acidic compartments containing proteases, as well as molecules promoting antigen presentation (see reference 21 for a recent review).Numerous proteins that are secreted from Mycobacterium have been described, and many of these have been postulated to contribute to the development of protective immunity (7,8,10,15,16,33,34). Surface proteins and proteins secreted by mycobacteria are likely preferential targets for the immune system early in infection. However, during chronic infection, in the absence of cell lysis and dispersal of killed bacteria, it is not clear what antigens, if any, are processed and presented for recognition by T cells. Limited acidification of the mycobacterial phagosome and its anomalous distribution of lysosomal markers indicate that it is not an optimal compartment for antigen processing (5, 31). It has previously been shown that mycobacterial lipids are actively released from the mycobacterial phagosome and traffic within the endocytic network of the host macrophage (3, 35). Mycobacterial proteins may have the same fate, providing an alternate mechanism by which bacterial proteins may intersect the antigen-processing pathway of the macrophage. ...

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Effect of Zinc Deficiency on the Appearance of Two Immunodominant Protein Antigens (32 kDa and 65 kDa) in Culture Filtrates of Mycobacteria

Cited by 26 publications

References 16 publications

Differential Expression of a Mycobacterium tuberculosis Protein Recognized by a Mouse Monoclonal Antibody

Differential Expression of a Mycobacterium tuberculosis Protein Recognized by a Mouse Monoclonal Antibody

Humoral response against heat shock proteins and other mycobacterial antigens after intravesical treatment with bacille Calmette–Guérin (BCG) in patients with superficial bladder cancer

Identification of Mycobacterial Surface Proteins Released into Subcellular Compartments of Infected Macrophages

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