Il Cristo in forma Pietatis del Rosso Fiorentino fra devozione e bellezza

<p>Differential distribution pattern of root- identified proteins in the four conditions described: TT, 42T, 42FS and 42RS.</p

Comprehensive Proteomic Analysis of <i>Trypanosoma cruzi</i> Epimastigote Cell Surface Proteins by Two Complementary Methods

<i>Trypanosoma cruzi</i> is a protozoan that causes Chagas’ disease, a neglected infectious illness that affects millions of people, mostly in Latin America. Here, the cell surface subproteome of the <i>T. cruzi</i> epimastigote life form was characterized. In order to prepare samples enriched in epimastigote plasma membrane protein, two distinct methodologies were optimized and evaluated. The first methodology was based on cell surface trypsinization (Shave) of intact living cells while the second approach used biotinylation of cell surface proteins followed by streptavidin affinity chromatography isolation of the labeled proteins. Both <i>T. cruzi</i> subproteomes were analyzed by LC-MS/MS. The results showed that the methodologies offered comprehensive and complementary information about the parasite’s plasma membrane subproteome

Cell Surface Proteome Analysis of Human-Hosted <i>Trypanosoma cruzi</i> Life Stages

Chagas’ disease is a neglected infectious illness, caused by the protozoan <i>Trypanosoma cruzi.</i> It remains a challenging health issue in Latin America, where it is endemic, and so far there is no immunoprophylatic vaccine or satisfactory chemotherapic treatment for its chronic stage. The present work addressed the analysis of the plasma membrane (PM) subproteome from <i>T. cruzi</i> human-hosted life stages, trypomastigote and axenic amastigote, by two complementary PM protein enrichment techniques followed by identification using an LC–MS/MS approach. The results revealed an extensive repertoire of proteins in the PM subproteomes, including enzymes that might be suitable candidates for drug intervention. The comparison of the cell surface proteome among the life forms revealed some potentially stage-specific enzymes, although the majority was shared by both stages. Bioinformatic analysis showed that the vast majority of the identified proteins are membrane-derived and/or possess predicted transmembrane domains. They are mainly involved in host cell infection, protein adhesion, cell signaling, and the modulation of mammalian host immune response. Several virulence factors and proteins potentially capable of acting at a number of metabolic pathways of the host and also to regulate cell differentiation of the parasite itself were also found

Four-way Venn diagrams comparing common spots with differential expression in TT, 42T, 42FS and 42RS conditions by ANOVA, considering p≤0.05 in (A) leaves and (B) roots of bean.

<p>Four-way Venn diagrams comparing common spots with differential expression in TT, 42T, 42FS and 42RS conditions by ANOVA, considering p≤0.05 in (A) leaves and (B) roots of bean.</p

List of <i>P. vulgaris</i> root proteins, identified by MS analysis.

<p>List of <i>P. vulgaris</i> root proteins, identified by MS analysis.</p

Differential distribution pattern of leaf- identified proteins in the four conditions described: TT, 42T, 42FS and 42RS.

<p>Differential distribution pattern of leaf- identified proteins in the four conditions described: TT, 42T, 42FS and 42RS.</p

RT-qPCR analysis of Chalcone isomerase (Chal), acyl-coA-binding protein (Ac), NAC1 domain protein (Nac), glyceraldehyde-3-phosphate dehydrogenase (Ghd) and PR1-like protein (Pr1)-enconding genes in roots of common bean plants challenged and unchallenged with <i>T. harzianum</i> ALL 42, <i>F. solani</i> and <i>R. solani</i>.

<p>(TT) unchallenged plants; 42T plants challenged with <i>T. harzianum</i> ALL 42; FS plants challenged with <i>F. solani</i>; RS plants challenged with <i>R. solani</i>; 42FS double challenged plants <i>T. harzianum</i> ALL 42 and F. solani; 42RS double challenged plants <i>T. harzianum</i> ALL 42 and <i>R. solani.</i> Time of growth: (A) 7, (B) 14 and (C) 21 days.</p

List of <i>P. vulgaris</i> leaf proteins, identified by MS analysis.

<p>List of <i>P. vulgaris</i> leaf proteins, identified by MS analysis.</p

Four-way Venn diagrams comparing exclusive spots in TT, 42T, 42FS and 42RS conditions by ANOVA, considering p≤0.05 in (A) leaves and (B) roots of bean.

<p>Four-way Venn diagrams comparing exclusive spots in TT, 42T, 42FS and 42RS conditions by ANOVA, considering p≤0.05 in (A) leaves and (B) roots of bean.</p

Functional categorization of <i>P. vulgaris</i> identified proteins.

<p>(A) Leaf tissue and (B) Root tissue.</p