Identification of a novel periplasmic catalase-peroxidase KatA of Legionella pneumophila

Amemura-Maekawa, J

doi:10.1016/s0378-1097(99)00254-2

Cited by 6 publications

(6 citation statements)

References 15 publications

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“…L. pneumophila contains two bifunctional catalase-peroxidases, KatA and KatB, Ϸ60% identical in nucleotide and amino acid sequence (3,6). Our studies show that, depending on the physiological function, KatA and KatB may be either redundant, overlapping, or independent.…”

Section: Discussionmentioning

confidence: 77%

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Catalase-Peroxidases of Legionella pneumophila : Cloning of the katA Gene and Studies of KatA Function

Bandyopadhyay

Steinman

2000

J Bacteriol

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Legionella pneumophila, the causative organism of Legionnaires' pneumonia, contains two enzymes with catalatic and peroxidatic activity, KatA and KatB. To address the issue of redundant, overlapping, or discrete in vivo functions of highly homologous catalase-peroxidases, the gene for katA was cloned and its function was studied in L. pneumophila and Escherichia coli and compared with prior studies of katB in this laboratory. katA is induced during exponential growth and is the predominant peroxidase in stationary phase. When katA is inactivated, L. pneumophila is more sensitive to exogenous hydrogen peroxide and less virulent in the THP-1 macrophage cell line, similar to katB. Catalatic-peroxidatic activity with different peroxidatic cosubstrates is comparable for KatA and KatB, but KatA is five times more active towards dianisidine. In contrast with these examples of redundant or overlapping function, stationary-phase survival is decreased by 100-to 10,000-fold when katA is inactivated, while no change from wild type is seen for the katB null. The principal clue for understanding this discrete in vivo function was the demonstration that KatA is periplasmic and KatB is cytosolic. This stationary-phase phenotype suggests that targets sensitive to hydrogen peroxide are present outside the cytosol in stationary phase or that the peroxidatic activity of KatA is critical for stationary-phase redox reactions in the periplasm, perhaps disulfide bond formation. Since starvation-induced stationary phase is a prerequisite to acquisition of virulence by L. pneumophila, further studies on the function and regulation of katA in stationary phase may give insights on the mechanisms of infectivity of this pathogen.

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Section: Discussionmentioning

confidence: 77%

“…Our results were consistent and additionally demonstrated the cytosolic location of KatB and quantitative data for intracellular locations. The presence of a signal peptide in L. pneumophila katA (3) and independent experiments by ourselves and others (3) establish the periplasmic location of KatA beyond a reasonable doubt.…”

Section: Resultsmentioning

confidence: 87%

Catalase-Peroxidases of Legionella pneumophila : Cloning of the katA Gene and Studies of KatA Function

Bandyopadhyay

Steinman

2000

J Bacteriol

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“…Whereas KatB is located exclusively in the bacterial cytosol, KatA possesses a signal peptide and is present in the periplasm of the bacterium. AmemuraMaekawa and coworkers proposed that the periplasmic catalase-peroxidase (KatA) protects L. pneumophila from oxidative stresses by inactivating the hydrogen peroxide converted from superoxide radicals by the action of SodC, a Cu-Znsuperoxide dismutase which is usually located in bacterial periplasm (1). Gene mutation experiments demonstrated that phagosomes containing L. pneumophila katA or katB mutant exhibited a higher frequency of colocalization with LAMP-1, and the bacterial mutants showed defective intracellular multiplication in primary macrophages and amoebae (2).…”

Section: Discussionmentioning

confidence: 99%

Identification, Recombinant Expression, Immunolocalization in Macrophages, and T-Cell Responsiveness of the Major Extracellular Proteins of Francisella tularensis

2006

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A safer and more effective vaccine than the previously developed live attenuated vaccine is needed for combating Francisella tularensis, a highly infectious bacterial pathogen. To search for potential candidates for inclusion in a new vaccine, we characterized the proteins present in the culture filtrates of a virulent recent clinical isolate and the attenuated live vaccine strain of F. tularensis using a proteomic approach. We identified a total of 12 proteins; among these, catalase-peroxidase was much more abundant in the culture filtrate of the virulent clinical isolate, whereas bacterioferritin was more abundant in the culture filtrate of the live vaccine strain. Streptolysin O treatment of infected human macrophages indicated that catalase-peroxidase and the heat shock protein GroEL are released intracellularly by actively growing F. tularensis. Mice immunized with F. tularensis developed significant cellmediated immune responses to catalase-peroxidase, the heat shock protein GroEL, and bacterioferritin as measured by splenic lymphocyte proliferation and gamma interferon production. Finally, we expressed the major culture filtrate proteins that are promising vaccine candidates in Escherichia coli at high levels in soluble form to facilitate study of their immunobiology and potential role in vaccines.

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“…The presence of two catalase-peroxidases that are ϳ60% identical in amino acid sequences (3,5) raises the question of whether these highly homologous isozymes are functionally redundant. We reported that both isozymes contribute to resistance to exogenous hydrogen peroxide.…”

Section: Discussionmentioning

confidence: 99%

Legionella pneumophila Catalase-Peroxidases Are Required for Proper Trafficking and Growth in Primary Macrophages

et al. 2003

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Legionella pneumophila, a parasite of aquatic amoebae and pathogen of pulmonary macrophages, replicates intracellularly, utilizing a type IV secretion system to subvert the trafficking of Legionella-containing phagosomes. Defense against host-derived reactive oxygen species has been proposed as critical for intracellular replication. Virulence traits of null mutants in katA and katB, encoding the two Legionella catalase-peroxidases, were analyzed to evaluate the hypothesis that L. pneumophila must decompose hydrogen peroxide to establish a replication niche in macrophages. Phagosomes containing katA or katB mutant Legionella colocalize with LAMP-1, a late endosomal-lysosomal marker, at twice the frequency of those of wild-type strain JR32 and show a decreased frequency of bacterial replication, in similarity to phenotypes of mutants with mutations in dotA and dotB, encoding components of the Type IV secretion system. Quantitative similarity of the katA/B phenotypes indicates that each contributes to virulence traits largely independently of intracellular compartmentalization (KatA in the periplasm and KatB in the cytosol). These data support a model in which KatA and KatB maintain a critically low level of H 2 O 2 compatible with proper phagosome trafficking mediated by the type IV secretion apparatus. During these studies, we observed that dotA and dotB mutations in wild-type strain Lp02 had no effect on intracellular multiplication in the amoeba Acanthamoeba castellanii, indicating that certain dotA/B functions in Lp02 are dispensable in that experimental model. We also observed that wild-type JR32, unlike Lp02, shows minimal contact-dependent cytotoxicity, suggesting that cytotoxicity of JR32 is not a prerequisite for formation of replication-competent Legionella phagosomes in macrophages.

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Identification of a novel periplasmic catalase-peroxidase KatA of Legionella pneumophila

Cited by 6 publications

References 15 publications

Catalase-Peroxidases of Legionella pneumophila : Cloning of the katA Gene and Studies of KatA Function

Catalase-Peroxidases of Legionella pneumophila : Cloning of the katA Gene and Studies of KatA Function

Identification, Recombinant Expression, Immunolocalization in Macrophages, and T-Cell Responsiveness of the Major Extracellular Proteins of Francisella tularensis

Legionella pneumophila Catalase-Peroxidases Are Required for Proper Trafficking and Growth in Primary Macrophages

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