Serological responses of patients with lepromatous and tuberculoid leprosy to 30-, 31-, and 32-kilodalton antigens of Mycobacterium tuberculosis

Rumschlag, H S; Shinnick, Thomas M.; Cohen, Mitchell L.

doi:10.1128/jcm.26.10.2200-2202.1988

Cited by 33 publications

(19 citation statements)

References 9 publications

(5 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…All of these latest results confirm and extend our previous data (19) and are in agreement with information recently published by others (8,21). On the other hand, a 32-kDa protein, isolated from BCG culture medium and identified as the A component of the BCG 85 complex, was shown to be immunodominant when antibodies were evaluated in active pulmonary TB (12).…”

Section: Discussionsupporting

confidence: 92%

Serology and leprosy: immunoassays comparing immunoglobulin G antibody responses to 28- and 30-kilodalton proteins purified from Mycobacterium bovis BCG

et al. 1991

View full text Add to dashboard Cite

Two major proteins from Mycobacterium bovis BCG culture filtrates with molecular masses of 28 kDa (P28) and 30 kDa (P.), identified as components of the BCG 85 complex, were purified and used in enzyme-linked immunosorbent assays (ELISAs) for the determination of specific immunoglobulin G (IgG) levels in patients with leprosy or tuberculosis or with exposure to these diseases. High reactivity to both antigens was observed with sera from lepromatous leprosy patients, whereas antibody levels in sera from paucibacillary leprosy patients were not significantly different from those in sera from healthy individuals from an area in which leprosy is endemic. High IgG responses were also found in some contacts of lepromatous leprosy patients. A comparison of the levels of anti-P28 and anti-P30 within the multibacillary leprosy patient group showed much higher IgG reactivity to P28 than to P30, suggesting that the antibody response of lepromatous patients is directed predominantly against the 28-kDa protein. A high degree of correlation in values of ELISAs based on P2. and on the phenolic glycolipid of Mycobacterium leprae was observed in all groups analyzed. The potential use of an assay based on the 28-kDa protein to selectively distinguish individuals destined to develop multibacillary leprosy is discussed, as also is the likelihood that the 28-kDa-30-kDa complex, part of the fibronectin-binding family, is an important component of M. leprae.

show abstract

Section: Discussionsupporting

confidence: 92%

Serology and leprosy: immunoassays comparing immunoglobulin G antibody responses to 28- and 30-kilodalton proteins purified from Mycobacterium bovis BCG

et al. 1991

View full text Add to dashboard Cite

show abstract

“…Proteins in the antigen 85 complex have emerged as important antigens in the host response to mycobacteria. Initially, the antigen 85 complex as a whole and then its individual components were found to react with sera from both TB and leprosy patients (29,35). Recent studies have established that purified components, in particular, M. tuberculosis 85A or P32 and M. bovis 85B, are potent T-cell antigens stimulating lymphocyte proliferation and gamma interferon release in TB patients (14,16).…”

Section: Discussionmentioning

confidence: 99%

T-cell determinants and antibody binding sites on the major mycobacterial secretory protein MPB59 of Mycobacterium bovis

et al. 1994

View full text Add to dashboard Cite

Among the first proteins encountered by the host immune system upon infection or vaccination with mycobacteria are those secreted by the bacillus during growth. The antigen 85 complex of Mycobacterium bovis bacillus Calmette-Guerin (BCG) is composed of three closely related members. The mature 85B protein of M. bovis (MPB59) has a high degree of amino acid identity with the M. bovis 85A protein (76%) and the Mycobacterium tuberculosis 85B (99%o) and 85A (76%) proteins. We have examined the regions of MPB59 which stimulate human T-and B-cell responses by use of a set of 28 synthetic peptides, 20 amino acids (aa) in length and overlapping by 10 aa. Initial proliferative assays with recombinant MPB59 demonstrated that peripheral blood mononuclear cells from 95% of BCG vaccinees and 52% of tuberculosis patients responded to the whole mature protein. Peripheral blood mononuclear cells from MPB59 responders, but not nonresponders, were stimulated by peptides in a dose-dependent fashion. Five peptides were reactive in more than half of the MPB59 responders. The T-cell-reactive regions were essentially identical in the M. bovis and M. tuberculosis 85B proteins. Subjects with a variety of HLA-DR phenotypes responded to a number of these peptides. The dominant T-cell-reactive regions were distinct from the peptides recognized by sera from tuberculosis patients (aa 71 to 100) and the murine monoclonal antibody HYT27 (aa 61 to 90). The region reactive with antibodies overlapped part of the MPB59 sequence recently shown to participate in the binding of MPB59 to fibronectin. . MATERIALS AND METHODSAntigens. (i) Recombinant MPB59 protein. A 974-bp fragment encoding the gene sequence for the mature MPB59 protein (20) was generated by PCR from M. bovis (strain AN5) chromosomal DNA, cloned into the BamHI and SmaI sites in the pGEX-2T vector (33), and expressed in Escherichia coli JM109. The recombinant protein, expressed as a fusion product with glutathione S-transferase (GST), was purified from cell sonicate by affinity chromatography with glutathione agarose, and the MPB59 protein was cleaved from the GST 5319 on August 6, 2020 by guest http://iai.asm.org/ Downloaded from

show abstract

“…Twenty-five patienis had received anti-tuberculous chetnothcrapy for at least (Stnonths, Serum was obtained from the remaining patients before initiating treatment. A total of 55 serum samples was obtained from seleeied patients with polar lepromatous (43) or tuberctiloid leprosy (12); patients were classified according to well-established criteria [6], Thirly-onc sera came from patients attending the Hospital Carrasco in Rosario. Argentina, and 26 were from Mexican individuals living in the San Luis Potosi area.…”

Section: Bacleriiim and Antigensmentioning

confidence: 99%

High antibody levels to the mycobacterial fibronectin-binding antigen of 30–31 kD in tuberculosis and lepromatous leprosy

Espitia

Sciutto

González‐Amaro³

et al. 1992

Clinical and Experimental Immunology

View full text Add to dashboard Cite

SUMMARYImmunoblot assays showed that mycobacterial fibronectin-binding antigens are important targets of the humoral immune response in tuberculosis and leprosy. Using culture filtrate antigens of Mycotxuterium tuhcrcuto.sis. strong reactivitv with lhe tibronectin-binding of 30 31 kD (l-'n 30-31) was demonstrated in 55-9'!^. of tuberculosis sera and in 56-5'^A of lepromatous leprosy sera. Sera from patients with lubcrculoid leprosy and control sera gave very weak binding. Reactivity of tuberculosis and lepromatous leprosy sera with the fibronectin-binding antigen of 58-60 kD(Fn 5S 60) was less conspicuous. The ability to rcuci with fibroncctin of the anligcns of 58 60 and 30 3! kD was demonstrated by parallel labelling wilh a fibronectin biotin conjugate. Fn 30 31 was purified to homogeneity by a two-step procedure and used for ELISA, Positive titres were found in 63^, out of 65 tuberculosis sera and in 60 5"o out of 43 lepromatous leprosy sera. Antibody titres in lepromatous leprosy sera were higher than in tuberculosis sera. Our observations indicate indirectly that M. tepiae possess a highly immunogenic molecule homologous to M. tiihcrcutosis Fn 30-31, which elicits a high antibody response in leproniaious leprosy but not in tuberculoid leprosy. In this investigation, direct evidence for the presence of this antigen in M. leprae was obtained by immunochemistry of lepromatous leprosy lesions with a mono.specifk aniibody raised against .M. tuberculosis Fn 30 31,

show abstract

Serological responses of patients with lepromatous and tuberculoid leprosy to 30-, 31-, and 32-kilodalton antigens of Mycobacterium tuberculosis

Cited by 33 publications

References 9 publications

Serology and leprosy: immunoassays comparing immunoglobulin G antibody responses to 28- and 30-kilodalton proteins purified from Mycobacterium bovis BCG

Serology and leprosy: immunoassays comparing immunoglobulin G antibody responses to 28- and 30-kilodalton proteins purified from Mycobacterium bovis BCG

T-cell determinants and antibody binding sites on the major mycobacterial secretory protein MPB59 of Mycobacterium bovis

High antibody levels to the mycobacterial fibronectin-binding antigen of 30–31 kD in tuberculosis and lepromatous leprosy

Contact Info

Product

Resources

About