Polyamines in growth and dimorphism of Paracoccidioides brasiliensis

San-Blas, G.; San-Blas, Felipe; Sorais, Fran&#x000E7;oise; Moreno, Belisario; Ruiz-Herrera, Jos&#x000E9;

doi:10.1007/s002030050404

Cited by 9 publications

(6 citation statements)

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“…Knowing that a transient increase in both the level of polyamines and the activity of polyamine synthetic enzymes characterizes the yeast-to-hypha transition in many fungal species (33,38,42,57,76), we hypothesized that overexpression of SAMDC could result in PHG in S. cerevisiae. To test this hypothesis, we increased the SPE2 copy number in strain W303-1b as a means to enhance SAMDC activity.…”

Section: Htpb Reaches the Cytosol Of L Pneumophila-infected Cellsmentioning

confidence: 99%

“…By definition, these compounds have more than one amino group and are commonly synthesized using amino acids as precursors (18,65). Based on the fact that a strong correlation exists between elevated polyamine levels and fungal filamentation (33,38,42,57,76), it seems reasonable to surmise that the activation of PHG by HtpB, via its interaction with SAMDC, is mediated by increased concentrations of intracellular polyamines in S. cerevisiae. In this view, it is predicted that yeast cells expressing HtpB would have elevated levels of spermidine and spermine.…”

Section: Htpb Reaches the Cytosol Of L Pneumophila-infected Cellsmentioning

confidence: 99%

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Legionella pneumophilaRequires Polyamines for Optimal Intracellular Growth

et al. 2011

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The Gram-negative intracellular pathogen Legionella pneumophila replicates in a membrane-bound compartment known as the Legionella-containing vacuole (LCV), into which it abundantly releases its chaperonin, HtpB. To determine whether HtpB remains within the LCV or reaches the host cell cytoplasm, we infected U937 human macrophages and CHO cells with L. pneumophila expressing a translocation reporter consisting of the Bordetella pertussis adenylate cyclase fused to HtpB. These infections led to increased cyclic AMP levels, suggesting that HtpB reaches the host cell cytoplasm. To identify potential functions of cytoplasmic HtpB, we expressed it in the yeast Saccharomyces cerevisiae, where HtpB induced pseudohyphal growth. A yeast-twohybrid screen showed that HtpB interacted with S-adenosylmethionine decarboxylase (SAMDC), an essential yeast enzyme (encoded by SPE2) that is required for polyamine biosynthesis. Increasing the copy number of SPE2 induced pseudohyphal growth in S. cerevisiae; thus, we speculated that (i) HtpB induces pseudohyphal growth by activating polyamine synthesis and (ii) L. pneumophila may require exogenous polyamines for growth. A pharmacological inhibitor of SAMDC significantly reduced L. pneumophila replication in L929 mouse cells and U937 macrophages, whereas exogenously added polyamines moderately favored intracellular growth, confirming that polyamines and host SAMDC activity promote L. pneumophila proliferation. Bioinformatic analysis revealed that most known enzymes required for polyamine biosynthesis in bacteria (including SAMDC) are absent in L. pneumophila, further suggesting a need for exogenous polyamines. We hypothesize that HtpB may function to ensure a supply of polyamines in host cells, which are required for the optimal intracellular growth of L. pneumophila.Chaperonins constitute a family of highly conserved proteins found in all prokaryotic and eukaryotic organisms (34). Their primary role is to facilitate the folding of nascent and stressdenatured proteins into their functional native states in an ATP-dependent manner (54). Group I chaperonins, referred to as Hsp60, Cpn60, or GroEL, are prokaryotic proteins found in bacteria and in eukaryotic organelles such as mitochondria and chloroplasts (34). Group II chaperonins, also known as CCT or TCP-1, are found in the eukaryotic cytosol and in the archaea (34). Structural and functional studies of Escherichia coli GroEL have established the role of group I chaperonins as intracellular mediators of protein folding (7, 94). GroEL is an essential protein in E. coli (23) whose intracellular level increases substantially in response to defined stressful stimuli (55, 85). The protein-folding paradigm of group I chaperonins has changed with accumulating reports of surface-and membrane-associated chaperonins that perform other diverse functions. For instance, the extracytoplasmically localized chaperonins of Haemophilus ducreyi (25), Helicobacter pylori (9, 92), Borrelia burgdorferi (77), and Clostridium difficile (37) have been implica...

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Section: Htpb Reaches the Cytosol Of L Pneumophila-infected Cellsmentioning

confidence: 99%

Section: Htpb Reaches the Cytosol Of L Pneumophila-infected Cellsmentioning

confidence: 99%

Legionella pneumophilaRequires Polyamines for Optimal Intracellular Growth

et al. 2011

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“…In T. vaginalis the putrescine formed by ODC is not metabolized further but is exported with the simultaneous uptake of spermine. 1,4-Diamino-2-butanone (DAB) is a competitive inhibitor of ODC in several cells (22,24). In several yeast and fungal cell lines it has been shown that depletion of intracellular polyamines by DAB prevents dimorphic transition without affecting growth (9,14).…”

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confidence: 99%

Inhibition of Polyamine Synthesis Arrests Trichomonad Growth and Induces Destruction of Hydrogenosomes

Reis

Martinez

Yarlett

et al. 1999

Antimicrob Agents Chemother

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Trichomonad parasites such as Tritrichomonas foetusproduce large amounts of putrescine (1,4-diaminobutane), which is transported out of the cell via an antiport mechanism which results in the uptake of a molecule of spermine. The importance of putrescine to the survival of the parasite and its role in the biology of T. foetus was investigated by use of the putrescine analogue 1,4-diamino-2-butanone (DAB). Growth of T. foetus in vitro was significantly inhibited by 20 mM DAB, which was reversed by the addition of exogenous 40 mM putrescine. High-performance liquid chromatography analysis of 20 mM DAB-treated T. foetusrevealed that putrescine, spermidine, and spermine levels were reduced by 89, 52, and 43%, respectively, compared to those in control cells. The DAB treatment induced several ultrastructural alterations, which were primarily observed in the redox organelles termed hydrogenosomes. These organelles were progressively degraded, giving rise to large vesicles that displayed material immunoreactive with an antibody to β-succinyl-coenzyme A synthetase, a hydrogenosomal enzyme. A protective role for polyamines as stabilizing agents in the trichomonad hydrogenosomal membrane is proposed.

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“…These are micromolecules required for cellular growth and differentiation in eukaryotic systems and originated by the decarboxylation of ornithine by ornithine decarboxylase (ODC), which gives rise to putrescine, the first polyamine in the metabolic pathway. In P. brasiliensis , high levels of ODC activity are induced at the onset of the budding process during the yeast growth and during the mycelium-to-yeast transition in vitro [21, 22]. Also, the dimorphic transition can be repressed by the addition of the ODC inhibitor 1,4-diamino-2-butanone (DAB) [22].…”

Section: Adaptationmentioning

confidence: 99%

“…In P. brasiliensis , high levels of ODC activity are induced at the onset of the budding process during the yeast growth and during the mycelium-to-yeast transition in vitro [21, 22]. Also, the dimorphic transition can be repressed by the addition of the ODC inhibitor 1,4-diamino-2-butanone (DAB) [22]. …”

Section: Adaptationmentioning

confidence: 99%

ParacoccidioidesSpp.: Virulence Factors and Immune-Evasion Strategies

Camacho

Niño-Vega

2017

Mediators of Inflammation

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Paracoccidioides spp. are dimorphic fungal pathogens responsible for one of the most relevant systemic mycoses in Latin America, paracoccidioidomycosis (PCM). Their exact ecological niche remains unknown; however, they have been isolated from soil samples and armadillos (Dasypus novemcinctus), which have been proposed as animal reservoir for these fungi. Human infection occurs by inhalation of conidia or mycelia fragments and is mostly associated with immunocompetent hosts inhabiting and/or working in endemic rural areas. In this review focusing on the pathogen perspective, we will discuss some of the microbial attributes and molecular mechanisms that enable Paracoccidioides spp. to tolerate, adapt, and ultimately avoid the host immune response, establishing infection.

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Polyamines in growth and dimorphism of Paracoccidioides brasiliensis

Cited by 9 publications

References 0 publications

Legionella pneumophilaRequires Polyamines for Optimal Intracellular Growth

Legionella pneumophilaRequires Polyamines for Optimal Intracellular Growth

Inhibition of Polyamine Synthesis Arrests Trichomonad Growth and Induces Destruction of Hydrogenosomes

ParacoccidioidesSpp.: Virulence Factors and Immune-Evasion Strategies

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