Extracellular and Cytosolic Iron Superoxide Dismutase from
            <i>Mycobacterium bovis</i>
            BCG

Kang, Suk‐Ku; Jung, Yong-Jae; Kim, Cheorl-Ho; Song, Chang Yong

doi:10.1128/cdli.5.6.784-789.1998

Cited by 13 publications

(8 citation statements)

References 31 publications

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“…Evidence of mycobacterial proteins changing subcellular location [ 31 ], may have an impact on the overall topographical classification of epitopes, and indicates the need to take experimental parameters into greater consideration. With this caveat in mind, the highest EDI 1 values for topology categories are seen in the extracelluar (11.49) and cytoplasmic (8.09) proteins (Figure 2b ).…”

Section: Resultsmentioning

confidence: 99%

An analysis of the epitope knowledge related to Mycobacteria

Blythe¹,

Zhang²,

Vaughan³

et al. 2007

Immunome Res

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Background: Tuberculosis, caused by the bacterium Mycobacterium tuberculosis, remains a leading cause of infectious disease morbidity and mortality, and is responsible for more than 2 million deaths a year. Reports about extremely drug resistant (XDR) strains have further heightened the sense of urgency for the development of novel strategies to prevent and treat TB. Detailed knowledge of the epitopes recognized by immune responses can aid in vaccine and diagnostics development, and provides important tools for basic research. The analysis of epitope data corresponding to M. tuberculosis can also identify gaps in our knowledge, and suggest potential areas for further research and discovery. The Immune Epitope Database (IEDB) is compiled mainly from literature sources, and describes a broad array of source organisms, including M. tuberculosis and other Mycobacterial species.

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Section: Resultsmentioning

confidence: 99%

An analysis of the epitope knowledge related to Mycobacteria

Blythe¹,

Zhang²,

Vaughan³

et al. 2007

Immunome Res

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“…Certain species express Mn- or Fe-containing SODs that are secreted to help defend against the O 2 •– burst of the host. In some cases, the Mn or Fe-SOD can work together with SodC to maximize oxidative stress defense as has been shown in M. tuberculosis − and related Mycobacterium , , as well as in spores of Bacillus anthracis , the causative agent of anthrax . In other cases, the bacterium lacks an obvious SodC and the Mn- or Fe-SOD is the sole defense against extracellular O 2 •– .…”

Section: Bacterial Pathogensmentioning

confidence: 99%

Chemical Warfare at the Microorganismal Level: A Closer Look at the Superoxide Dismutase Enzymes of Pathogens

Schatzman

Culotta

2018

ACS Infect. Dis.

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Superoxide anion radical is generated as a natural byproduct of aerobic metabolism, but is also produced as part of the oxidative burst of the innate immune response design to kill pathogens. In living systems, superoxide is largely managed through superoxide dismutases (SODs), families of metalloenzymes that use Fe, Mn, Ni or Cu cofactors to catalyze the disproportionation of superoxide to oxygen and hydrogen peroxide. Given the bursts of superoxide faced by microbial pathogens, it comes as no surprise that SOD enzymes play important roles in microbial survival and virulence. Interestingly, microbial SOD enzymes not only detoxify host superoxide, but may also participate in signaling pathways that involve reactive oxygen species derived from the microbe itself, particularly in the case of eukaryotic pathogens. In this review, we will discuss the chemistry of superoxide radicals and the role of diverse SOD metalloenzymes in bacterial, fungal, and protozoan pathogens. We will highlight the unique features of microbial SOD enzymes that have evolved to accommodate the harsh lifestyle at the host-pathogen interface. Lastly, we will discuss key non-SOD superoxide scavengers that specific pathogens employ for defense against host superoxide.

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“…Although most studies propose a cytoplasmic location for SODs, their secretion by some organisms, such as Mycobacterium avium and M . bovis BCG, has been reported . In a former study, we found that FeSOD is immunogenic in the surface immunoproteome of B. pertussis .…”

Section: Discussionmentioning

confidence: 64%

“…The function of SODs is to scavenge superoxide radicals to molecular oxygen or hydrogen peroxide in order to protect organisms against oxidative stress (32). Although most studies propose a cytoplasmic location for SODs, their secretion by some organisms, such as Mycobacterium avium and M. bovis BCG, has been reported (32,33). In a former study, we found that FeSOD is immunogenic in the surface immunoproteome of B. pertussis (15).…”

Section: Discussionmentioning

confidence: 89%

Immunogenicity and protective efficacy of recombinant iron superoxide dismutase protein from Bordetella pertussis in mice models

Yılmaz

Apak

Özcengīz

et al. 2016

Microbiology and Immunology

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Whooping cough (pertussis) is a highly contagious respiratory infection caused by Bordetella pertussis. Although availability of effective pertussis vaccines reportedly decreases the incidence of the disease, B. pertussis circulation in populations has not been eliminated. Thus, it is necessary to find new protein candidates with greater immune protective capacities than the currently available acellular pertussis vaccines. In this study, iron superoxide dismutase (FeSOD) gene (sodB) was cloned, expressed in Escherichia coli and recombinant FeSOD protein thence purified. The recombinant protein (rFeSOD) was formulated with aluminum hydroxide (Alum) or monophosphoryl lipid A (MPLA) and injected intraperitoneally to immunize mice, after which IgG1, IgG2a and IFN-g titers were measured to assess humoral and cellular responses, respectively, to these immunizations. The extent of bacterial colonization in lungs of intranasally challenged mice was determined 5, 8 and 14 days post-challenge. IgG1 and IgG2a responses were significantly stronger in mice that had been immunized with rFeSOD-MPLA than in those that had received rFeSOD-Alum (P < 0.05). Additionally, IgG2a titers were higher in mice vaccinated with recombinant protein FeSOD (rFeSOD) formulated with MPLA, especially after the second immunization. Immunization with rFeSOD-MPLA also provided a modest, but significant decrease in bacterial counts in lungs of mice (P < 0.05). Antigen specific-IFN-g responses were significantly stronger in the group vaccinated with rFeSOD-MPLA, which could account for the lower bacterial counts. These findings suggest that rFeSOD protein formulated with MPLA has potential as an acellular pertussis vaccine candidate component.

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Extracellular and Cytosolic Iron Superoxide Dismutase from Mycobacterium bovis BCG

Cited by 13 publications

References 31 publications

An analysis of the epitope knowledge related to Mycobacteria

An analysis of the epitope knowledge related to Mycobacteria

Chemical Warfare at the Microorganismal Level: A Closer Look at the Superoxide Dismutase Enzymes of Pathogens

Immunogenicity and protective efficacy of recombinant iron superoxide dismutase protein from Bordetella pertussis in mice models

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