The GroES antigens of Mycobacterium avium and Mycobacterium paratuberculosis

Cobb, Alison J; Frothingham, Richard

doi:10.1016/s0378-1135(99)00019-x

Cited by 25 publications

(15 citation statements)

References 19 publications

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“…paratuberculosis. Among these are the heat shock proteins GroES (9) and GroEL (14), 2 alkyl hydroperoxide reductases (25), a serine protease (6), superoxide dismutase (21), and 11 other proteins of unknown function that are named on the basis of their sizes in kilodaltons (3, 10, 13, 15, 16, 23, 24, 26-28, 33, 37). Some of these antigens appear to show promise, but none has been incorporated as a routine diagnostic tool according to the published literature and available commercial tests.…”

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Expression and Immunogenicity of Proteins Encoded by Sequences Specific to Mycobacterium avium subsp. paratuberculosis

et al. 2004

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The development of immunoassays specific for the diagnosis of Johne's disease in cattle requires antigens specific to Mycobacterium avium subsp. paratuberculosis. However, because of genetic similarity to other mycobacteria comprising the M. avium complex, no such antigens have been found. Through a comparative genomics approach, 21 potential coding sequences of M. avium subsp. paratuberculosis that are not represented in any other mycobacterial species tested (n ‫؍‬ 9) were previously identified (

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Expression and Immunogenicity of Proteins Encoded by Sequences Specific to Mycobacterium avium subsp. paratuberculosis

et al. 2004

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“…paratuberculosis and Mycobacterium avium subsp. avium are antigenically and genetically very similar organisms (8,21). Despite considerable study, clear antigenic differences between the organisms have not been identified; at the nucleotide level, the two organisms are 99.6% conserved (14,21).…”

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Regulation of Expression of Major Histocompatibility Antigens by Bovine Macrophages Infected withMycobacterium aviumsubsp.paratuberculosisorMycobacterium aviumsubsp.avium

et al. 2001

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Mycobacterium avium subsp. paratuberculosis and Mycobacterium avium subsp. avium are antigenically and genetically very similar organisms; however, they differ markedly in their virulence for cattle. We evaluated the capacity of bovine macrophages infected with M. avium subsp. paratuberculosis or M. avium subsp. avium to express major histocompatibility complex (MHC) class I and class II antigens on their surface and to interact with primed autologous lymphocytes. Our results indicate that infection of bovine macrophages with M. avium subsp. paratuberculosis promoted the downregulation of MHC class I and class II molecules on the macrophage surface within 24 and 12 h, respectively. Alternatively, MHC class II expression by M. avium subsp. aviuminfected macrophages was not detected until 24 h after infection, and the magnitude of the decrease was smaller. Decreased MHC class I expression by M. avium subsp. avium-infected macrophages was not detected. Unlike M. avium subsp. paratuberculosis-infected macrophages, M. avium subsp. avium-infected macrophages upregulated MHC class I and class II expression after activation by gamma interferon or tumor necrosis factor alpha. Further, M. avium subsp. avium-infected macrophages were lysed by primed autologous lymphocytes, whereas M. avium subsp. paratuberculosis-infected macrophages were not. Overall, the results support the hypothesis that the difference in the virulence of M. avium subsp. paratuberculosis and M. avium subsp. avium for cattle is dependent on a difference in the capacity of the organisms to suppress mycobacterial antigen presentation to T lymphocytes.

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“…Spot CS12-5.13 was identified as a 10-kDa chaperonin M. paratuberculosis protein (also called GroES or HSP10) (15,23), and spot CS29-5.51 was confirmed to be fibronectin-binding antigen 85 complex B (also called Ag85B) (18). Spot CS29-5.37 was identified as an M. avium alpha antigen protein.…”

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Possible Association of GroES and Antigen 85 Proteins with Heat Resistance ofMycobacterium paratuberculosis

Sung¹,

Takayama

Collins³

2004

Appl Environ Microbiol

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Conflicting reports on the heat resistance of Mycobacterium paratuberculosis prompted an examination of the effect of culture medium on this property of the organism. M. paratuberculosis was cultured in three types of media (fatty acid-containing medium 7H9-OADC (oleic acid-albumin-dextrose-catalase supplement) and glycerol-containing media WR-GD and 7H9-GD [glycerol-dextrose supplement]) at pH 6.0. M. paratuberculosis grown under these three culture conditions was then tested for heat resistance in distilled water at 65°C. Soluble proteins and mycolic acids of M. paratuberculosis were evaluated by two-dimensional electrophoresis (2-DE) and thin-layer chromatography (TLC), respectively. The type of culture medium used significantly affected the heat resistance of M. paratuberculosis. The decimal reduction times at 65°C (D 65°C values; times required to reduce the concentration of bacteria by a factor of 10 at 65°C) for M. paratuberculosis strains grown in 7H9-OADC were significantly higher than those for the organisms grown in WR-GD medium (P < 0.01). When the glycerol-dextrose supplement of WR was substituted for the fatty acid supplement (OADC) in 7H9 medium (resulting in 7H9-GD), the D 65°C value was significantly lower than that for the organism grown in 7H9-OADC medium (P ‫؍‬ 0.022) but higher than that when it was cultured in WR-GD medium (P ‫؍‬ 0.005). Proteomic analysis by 2-DE of soluble proteins extracted from M. paratuberculosis grown without heat stress in the three media (7H9-OADC, 7H9-GD, and WR-GD) revealed that seven proteins were more highly expressed in 7H9-OADC medium than in the other two media. When the seven proteins were subjected to matrix-assisted laser desorption ionization-mass spectrometric analysis, four of the seven protein spots were unidentifiable. The other three proteins were identified as GroES heat shock protein, alpha antigen, and antigen 85 complex B (Ag85B; fibronectin-binding protein). These proteins may be associated with the heat resistance of M. paratuberculosis. Alpha antigen and Ag85B are both trehalose mycolyltransferases involved in mycobacterial cell wall assembly. TLC revealed that 7H9-OADC medium supported production of more trehalose dimycolates and cell wall-bound mycolic acids than did WR-GD medium. The present study shows that in vitro culture conditions significantly affect heat resistance, cell wall synthesis, and protein expression of M. paratuberculosis and emphasize the importance of culture conditions on in vitro and ex vivo studies to estimate heat resistance.Mycobacterium paratuberculosis (also known as Mycobacterium avium subsp. paratuberculosis) is the cause of Johne's disease in animals, in particular dairy cattle (14). Numerous studies report a significant association of this pathogen with the chronic inflammatory bowel disease of humans called Crohn's disease (10,17,21,45,50). Consequently, M. paratuberculosis has come under scrutiny as a potential food-borne pathogen of dairy products (16). For this reason, studies of M. paratuberculosis heat re...

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The GroES antigens of Mycobacterium avium and Mycobacterium paratuberculosis

Cited by 25 publications

References 19 publications

Expression and Immunogenicity of Proteins Encoded by Sequences Specific to Mycobacterium avium subsp. paratuberculosis

Expression and Immunogenicity of Proteins Encoded by Sequences Specific to Mycobacterium avium subsp. paratuberculosis

Regulation of Expression of Major Histocompatibility Antigens by Bovine Macrophages Infected withMycobacterium aviumsubsp.paratuberculosisorMycobacterium aviumsubsp.avium

Possible Association of GroES and Antigen 85 Proteins with Heat Resistance ofMycobacterium paratuberculosis

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