Actividades de crianças do pré-escolar e educadores de infância com o computador em portugal

Muito se tem escrito hoje sobre a integração das tecnologias de informação e comunicação (TIC) na escola e diversas pesquisas têm vindo a demonstrar a importância da familiarização da criança desta idade com a tecnologia, quer porque esta faz parte inquestionável do mundo que a rodeia, quer pela relevância educativa das experiências que lhe pode proporcionar. No entanto existem muito poucos estudos que nos descrevam e analisem processos efectivos de integração da tecnologia na Escola em geral, e ao nível da educação Pré-Escolar em particular. Este foi o ponto de partida da nossa investigação, verificar as práticas de crianças e Educadores de Infância com as TIC, mais especificamente o computador, em Portugal. Elaborámos um questionário que foi enviado, via correio electrónico, para Educadores de Infância de todo o país e como forma de triangulação de dados foram realizadas observações em dois jardins-de-infância, mais concretamente nas aulas de informática das crianças do pré-escolar. Terminamos com conclusões baseadas nos dados recolhidos e algumas considerações finais sobre o tema

Lipidomic Analysis of Extracellular Vesicles from the Pathogenic Phase of Paracoccidioides brasiliensis

Background: Fungal extracellular vesicles are able to cross the cell wall and transport molecules that help in nutrient acquisition, cell defense, and modulation of the host defense machinery.Methodology/Principal Findings: Here we present a detailed lipidomic analysis of extracellular vesicles released by Paracoccidioides brasiliensis at the yeast pathogenic phase. We compared data of two representative isolates, Pb3 and Pb18, which have distinct virulence profiles and phylogenetic background. Vesicle lipids were fractionated into different classes and analyzed by either electrospray ionization- or gas chromatography-mass spectrometry. We found two species of monohexosylceramide and 33 phospholipid species, including phosphatidylcholine, phosphatidylethanolamine, phosphatidic acid, phosphatidylserine, phosphatidylinositol, and phosphatidylglycerol. Among the phospholipid-bound fatty acids in extracellular vesicles, C181 predominated in Pb3, whereas C18:2 prevailed in Pb18. the prevalent sterol in Pb3 and Pb18 vesicles was brassicasterol, followed by ergosterol and lanosterol. Inter-isolate differences in sterol composition were observed, and also between extracellular vesicles and whole cells.Conclusions/Significance: the extensive lipidomic analysis of extracellular vesicles from two P. brasiliensis isolates will help to understand the composition of these fungal components/organelles and will hopefully be useful to study their biogenesis and role in host-pathogen interactions.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)National Institutes of Health (NIH)Universidade Federal de São Paulo, UNIFESP, Dept Microbiol Imunol & Parasitol, São Paulo, BrazilUniv Texas El Paso, Dept Biol Sci, Border Biomed Res Ctr, El Paso, TX 79968 USAUniversidade Federal de São Paulo, UNIFESP, Dept Microbiol Imunol & Parasitol, São Paulo, BrazilFAPESP: 06/05095-6FAPESP: 07/04757-8FAPESP: 07/59768-4CNPq: 301666/2010-5National Institutes of Health (NIH): 5G12RR008124-16A1National Institutes of Health (NIH): 5G12RR008124-16A1S1National Institutes of Health (NIH): G12MD007592Web of Scienc

Genome of the Avirulent Human-Infective Trypanosome—Trypanosoma rangeli

Background: Trypanosoma rangeli is a hemoflagellate protozoan parasite infecting humans and other wild and domestic mammals across Central and South America. It does not cause human disease, but it can be mistaken for the etiologic agent of Chagas disease, Trypanosoma cruzi. We have sequenced the T. rangeli genome to provide new tools for elucidating the distinct and intriguing biology of this species and the key pathways related to interaction with its arthropod and mammalian hosts.  Methodology/Principal Findings: The T. rangeli haploid genome is ,24 Mb in length, and is the smallest and least repetitive trypanosomatid genome sequenced thus far. This parasite genome has shorter subtelomeric sequences compared to those of T. cruzi and T. brucei; displays intraspecific karyotype variability and lacks minichromosomes. Of the predicted 7,613 protein coding sequences, functional annotations could be determined for 2,415, while 5,043 are hypothetical proteins, some with evidence of protein expression. 7,101 genes (93%) are shared with other trypanosomatids that infect humans. An ortholog of the dcl2 gene involved in the T. brucei RNAi pathway was found in T. rangeli, but the RNAi machinery is non-functional since the other genes in this pathway are pseudogenized. T. rangeli is highly susceptible to oxidative stress, a phenotype that may be explained by a smaller number of anti-oxidant defense enzymes and heatshock proteins.  Conclusions/Significance: Phylogenetic comparison of nuclear and mitochondrial genes indicates that T. rangeli and T. cruzi are equidistant from T. brucei. In addition to revealing new aspects of trypanosome co-evolution within the vertebrate and invertebrate hosts, comparative genomic analysis with pathogenic trypanosomatids provides valuable new information that can be further explored with the aim of developing better diagnostic tools and/or therapeutic targets

Comparative Genomic Analysis of Human Fungal Pathogens Causing Paracoccidioidomycosis

Paracoccidioides is a fungal pathogen and the cause of paracoccidioidomycosis, a health-threatening human systemic mycosis endemic to Latin America. Infection by Paracoccidioides, a dimorphic fungus in the order Onygenales, is coupled with a thermally regulated transition from a soil-dwelling filamentous form to a yeast-like pathogenic form. To better understand the genetic basis of growth and pathogenicity in Paracoccidioides, we sequenced the genomes of two strains of Paracoccidioides brasiliensis (Pb03 and Pb18) and one strain of Paracoccidioides lutzii (Pb01). These genomes range in size from 29.1 Mb to 32.9 Mb and encode 7,610 to 8,130 genes. To enable genetic studies, we mapped 94% of the P. brasiliensis Pb18 assembly onto five chromosomes. We characterized gene family content across Onygenales and related fungi, and within Paracoccidioides we found expansions of the fungal-specific kinase family FunK1. Additionally, the Onygenales have lost many genes involved in carbohydrate metabolism and fewer genes involved in protein metabolism, resulting in a higher ratio of proteases to carbohydrate active enzymes in the Onygenales than their relatives. To determine if gene content correlated with growth on different substrates, we screened the non-pathogenic onygenale Uncinocarpus reesii, which has orthologs for 91% of Paracoccidioides metabolic genes, for growth on 190 carbon sources. U. reesii showed growth on a limited range of carbohydrates, primarily basic plant sugars and cell wall components; this suggests that Onygenales, including dimorphic fungi, can degrade cellulosic plant material in the soil. In addition, U. reesii grew on gelatin and a wide range of dipeptides and amino acids, indicating a preference for proteinaceous growth substrates over carbohydrates, which may enable these fungi to also degrade animal biomass. These capabilities for degrading plant and animal substrates suggest a duality in lifestyle that could enable pathogenic species of Onygenales to transfer from soil to animal hosts.National Institute of Allergy and Infectious Diseases (U.S.)National Institutes of Health. Department of Health and Human Services (contract HHSN266200400001C)National Institutes of Health. Department of Health and Human Services(contract HHSN2722009000018C)Brazil. National Council for Scientific and Technological Developmen

Overall results of the I.D. and immunoblot reactivity of recombinant <i>P. lutzii</i> (rPlp43), native or recombinant gp43 (gp43, gp43r3) and their Endo H-deglycosylated forms (EH-gp43, EH-gp43r3) with PCM patients' sera from Brazilian Southeastern (S) and Midwestern (M) regions (Table S1).

<p>*Sera groups: 1, 1S–50S and 82M–95M; 2, 51M–81M; 3, 96M–98M.</p>#<p>ID titers with purified gp43 or Pb339 culture supernantant are specified in <a href="http://www.plosntds.org/article/info:doi/10.1371/journal.pntd.0003111#pntd.0003111.s002" target="_blank">Table S2</a>.</p><p>Overall results of the I.D. and immunoblot reactivity of recombinant <i>P. lutzii</i> (rPlp43), native or recombinant gp43 (gp43, gp43r3) and their Endo H-deglycosylated forms (EH-gp43, EH-gp43r3) with PCM patients' sera from Brazilian Southeastern (S) and Midwestern (M) regions (<a href="http://www.plosntds.org/article/info:doi/10.1371/journal.pntd.0003111#pntd.0003111.s001" target="_blank">Table S1</a>).</p

(A) Representative immunoblot reactions of PCM patients' sera (1∶1,000) with rPlp43 and Endo H-deglycosylated (EH-) gp43.

<p>The overall results are shown in <a href="http://www.plosntds.org/article/info:doi/10.1371/journal.pntd.0003111#pntd-0003111-t001" target="_blank">Table 1</a> for sera groups 1, 2, 3, and individual sera 99M, 100M, and101M. On the right, CBB-stained SDS-PAGE gel showing the amount of antigen used in the reactions. Results with Endo H-deglycosylated gp43r3 were similar to (EH-)gp43 and are not shown. (<b>B</b>) <b>PCR amplification of </b><i>HSP70</i><b> using primers for the </b><i>P. lutzii</i><b> gene as shown in an agarose gel.</b> Partial <i>HSP70</i> PCR (529 bp) amplification shows that clinical isolates Pb51M and Pb52M are <i>P. lutzii</i>. DNA extracted from Pb01 (<i>P. lutzii</i>) and Pb18 (<i>P. brasiliensis</i>) were used as species control. Crt-, in the absence of DNA.</p

Recombinant rPlp43 is not glycosylated and seems to be enzymatically active.

<p>(<b>A</b>) Heterologous expression of rPlp43 in <i>P. pastoris</i> culture supernatants from methanol-induced recombinant yeasts containing the Pl<i>P43</i> insert or not (EV, empty vector). (<b>B</b>) SDS-PAGE profile of rPlp43 and control gp43 before (−) and after (+) treatment with Endo H. (<b>C</b>) Glucanase activity against PNPG in culture supernatants from <i>P. pastoris</i> expressing rPlp43 when compared with that, at equivalent total protein amount, of yeasts containing empty vector (EV), wild type <i>P. pastoris</i> and <i>S. cerevisiae</i>. Purified gp43 was used as protein negative control at equivalent protein amount to rPlp43, as estimated in SDS-PAGE gels. BSA was also included as negative control at higher amounts. PBS+rPlp43 (without substrate) and PNPG+enzyme buffer (without substrate) were used as negative controls. Migration of standard molecular masses is indicated.</p