Bacteremia by colistin-resistant Acinetobacter baumannii isolate: a case report.

BACKGROUND: Carbapenem-resistant Acinetobacter baumannii infections are a major public health problem worldwide, requiring the use of "old" antibiotics such as polymyxin B and E (colistin). However, there is concern regarding the emergence of isolates resistant to these antibiotics. CASE PRESENTATION: We report a case of a 64-year-old mestizo man hospitalized in an intensive care unit of a health institution in Colombia with identification and clinical and molecular typing of a colistin- and carbapenem-resistant A. baumannii isolate with mechanisms of resistance to colistin not previously reported, causing bacteremia. CONCLUSIONS: We have identified a strain of A. baumannii with mechanisms of resistance to colistin not previously reported in a patient with bacteremia who required treatment with multiple antibiotic schemes and had an adequate response.

Understanding the Photocatalytic Properties of Pt/CeOx /TiO2 : Structural Effects on Electronic and Optical Properties.

Ceria-titania interfaces play a crucial role in different chemical processes but are especially promising for the photocatalytic splitting of water using light in the visible wavelength region when Pt is added to the system. However, the complexity of this hierarchical structure hampers the study of the origin of its outstanding properties. In this article, the structural, electronic and optoelectronic properties of CeO2 /TiO2 systems containing 1D, 2D, and 3D particles of ceria are analyzed by means of density functional calculations. Adsorption sites and vacancy effects have been studied to model Pt adsorption. Density of states calculations and absorption spectra simulations explain the behavior of these systems. Finally, these models are used for the screening of other metals that can be combined with this heterostructure to potentially find more efficient water splitting photocatalysts.

Eficacia del tratamiento con ondas de choque en las úlceras por calcinosis distrófica / Effectiveness of Extracorporeal Shock Wave Lithotripsy to Treat Dystrophic Calcinosis Cutis Ulcers

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Screening and characterization of Bacillus thuringiensis isolates from Brazil for the presence of coleoptera-specific cry genes.

Forty-three Bacillus thuringiensis isolates from Brazil and 3 from Argentina were screened, using the polymerase chain reaction (PCR), for various coleoptera-specific cry genes. Seven isolates produced specific and/or nonspecific DNA fragments in a PCR reaction with primers specific for two coleopteran cry genes and 4 of these produced DNA fragments with primers specific for 7 known coleopteran cry genes. These isolates showed, by electron microscopy, the presence of spherical crystals. They also showed proteins of around 70 kDa which were immunologically similar to the Cry3Aa protein from B. thuringiensis subsp. tenebrionis. The 3 isolates from Argentina were toxic to T. molitor, and although no isolate from Brazil showed toxicity, they might show toxicity to another insect species.

Increase of a calcium independent transglutaminase activity in the erythrocyte during the infection with Plasmodium falciparum.

We have studied the activity of a calcium dependent transglutaminase (EC 2.3.2.13) during the growth of the parasite Plasmodium falciparum inside the infected human erythrocyte. There is only one detectable transglutaminase in the two-cell-system, and its origin is erythrocytic. No activity was detected in preparations of the parasite devoid of erythrocyte cytoplasm. The Michaelis Menten constants (Km) of the enzyme for the substrates N'N' dimethylcaseine and putrescine were undistinguishable whether the cell extracts used in their determination were obtained from normal or from infected red cells. The total activity of transglutaminase in stringently synchronized cultures, measured at 0.5 mM Ca2+, decreased with the maturation of the parasite. However, a fraction which became irreversibly activated and independent of calcium concentration was detected. The proportion of this fraction grew with maturation; it represented only 20% of the activity in 20 hr-old-trophozoites while in 48-hr-schizonts it was more than 85% of the total activity. The activation of this fraction of transglutaminase did not depend on an increase in the erythrocyte cytoplasmic calcium, since most of the calcium was shown to be located in the parasite.

Both the catalytic and regulatory domains of protein kinase C chimeras modulate the proliferative properties of NIH 3T3 cells.

Protein kinase C (PKC) isozymes exhibit important differences in terms of their regulation and biological functions. Not only may some PKC isoforms be active and others not for a given response, but the actions of different isoforms may even be antagonistic. In NIH 3T3 cells, for example, PKCdelta arrests cell growth whereas PKCepsilon stimulates it. To probe the contribution of the regulatory and the catalytic domains of PKC isozymes to isozyme-specific responses, we prepared chimeras between the regulatory and the catalytic domains of PKCalpha, -delta, and -epsilon. These chimeras, which preserve the overall structure of the native PKC enzymes, were stably expressed in mouse fibroblasts. A major objective was to characterize the growth properties of the cells that overexpress the various PKC constructs. Our data demonstrate that both the regulatory and the catalytic domains play roles in cell proliferation. The regulatory domain of PKCepsilon enhanced cell growth in the absence or presence of phorbol 12-myristate 13-acetate (PMA), and, in the presence of PMA, all chimeras with the PKCepsilon regulatory domain also gave rise to colonies in soft agar; the role of the catalytic domain of PKCepsilon was evident in the PMA-treated cells that overexpressed the PKC chimera containing the delta regulatory and the epsilon catalytic domains (PKCdelta/epsilon). The important contribution of the PKCepsilon catalytic domain to the growth of PKCdelta/epsilon-expressing cells was also evident in terms of a significantly increased saturation density in the presence of PMA, their formation of foci upon PMA treatment, and the induction of anchorage-independent growth. Aside from the growth-promoting effect of PKCepsilon, we have shown that most chimeras with PKCalpha and -delta regulatory domains inhibit cell growth. These results underscore the complex contributions of the regulatory and catalytic domains to the overall behavior of PKC.

The catalytic domain of protein kinase C chimeras modulates the affinity and targeting of phorbol ester-induced translocation.

Emerging evidence suggests important differences among protein kinase C (PKC) isozymes in terms of their regulation and biological functions. PKC is regulated by multiple interdependent mechanisms, including enzymatic activation, translocation of the enzyme in response to activation, phosphorylation, and proteolysis. As part of our ongoing studies to define the factors contributing to the specificity of PKC isozymes, we prepared chimeras between the catalytic and regulatory domains of PKCalpha, -delta, and -epsilon. These chimeras, which preserve the overall structure of the native PKC enzymes, were stably expressed in NIH 3T3 fibroblasts. Their intracellular distribution was similar to that of the endogenous enzymes, and they responded with translocation upon treatment with phorbol 12-myristate 13-acetate (PMA). We found that the potency of PMA for translocation of the PKCalpha/x chimeras from the soluble fraction was influenced by the catalytic domain. The ED50 for translocation of PKCalpha/alpha was 26 nM, in marked contrast to the ED50 of 0.9 nM in the case of the PKCalpha/epsilon chimera. In addition to this increase in potency, the site of translocation was also changed; the PKCalpha/epsilon chimera translocated mainly into the cytoskeletal fraction. PKCx/epsilon chimeras displayed twin isoforms with different mobilities on Western blots. PMA treatment increased the proportion of the higher mobility isoform. The two PKCx/epsilon isoforms differed in their localization; moreover, their localization pattern depended on the regulatory domain. Our results emphasize the complex contributions of the regulatory and catalytic domains to the overall behavior of PKC.