Full Text Available CBRC-TTRU-01-0386 ref|ZP_05563533.1| PrgI [Enterococcus faecalis DS5] ref|ZP_05594643.1| PrgI [Enterococcus... faecalis AR01/DG] ref|YP_003329065.1| PrgI [Enterococcus faecalis] gb|EEU66490.1| PrgI [Enterococcus... faecalis DS5] gb|EEU89437.1| PrgI [Enterococcus faecalis AR01/DG] gb|ACY95541.1| PrgI [Enterococcus faecalis] ZP_05563533.1 2.7 34% ...
Full Text Available CBRC-TTRU-01-0386 ref|YP_195782.1| PrgI [Enterococcus faecalis] ref|ZP_03986097.1| PrgI family protein [Ente...rococcus faecalis HH22] ref|ZP_04648464.1| conserved hypothetical protein [Enterococcus... faecalis TUSoD Ef11] ref|ZP_05563853.1| PrgI [Enterococcus faecalis Merz96] gb|AAW51314.1| PrgI [Enterococcus... faecalis] gb|EEI55785.1| PrgI family protein [Enterococcus faecalis HH22] ...gb|EEQ21547.1| conserved hypothetical protein [Enterococcus faecalis TUSoD Ef11] gb|EEU66810.1| PrgI [Enterococcus faecalis Merz96] YP_195782.1 2.7 34% ...
Full Text Available Salmonella enterica species are enteric pathogens that cause severe diseases ranging from self-limiting gastroenteritis to enteric fever and sepsis in humans. These infectious diseases are still the major cause of morbidity and mortality in low-income countries, especially in children younger than 5 years and immunocompromised adults. Vaccines targeting typhoidal diseases are already marketed, but none protect against non-typhoidal Salmonella. The existence of multiple non-typhoidal Salmonella serotypes as well as emerging antibiotic resistance highlight the need for development of a broad-spectrum protective vaccine. All Salmonella spp. utilize two type III Secretion Systems (T3SS 1 and 2 to initiate infection, allow replication in phagocytic cells and induce systemic disease. T3SS-1, which is essential to invade epithelial cells and cross the barrier, forms an extracellular needle and syringe necessary to inject effector proteins into the host cell. PrgI and SipD form, respectively, the T3SS-1 needle and the tip complex at the top of the needle. Because they are common and highly conserved in all virulent Salmonella spp., they might be ideal candidate antigens for a subunit-based, broad-spectrum vaccine.We investigated the immunogenicity and protective efficacy of PrgI and SipD administered by subcutaneous, intranasal and oral routes, alone or combined, in a mouse model of Salmonella intestinal challenge. Robust IgG (in all immunization routes and IgA (in intranasal and oral immunization routes antibody responses were induced against both proteins, particularly SipD. Mice orally immunized with SipD alone or SipD combined with PrgI were protected against lethal intestinal challenge with Salmonella Typhimurium (100 Lethal Dose 50% depending on antigen, route and adjuvant.Salmonella T3SS SipD is a promising antigen for the development of a protective Salmonella vaccine, and could be developed for vaccination in tropical endemic areas to control
ANTAGONISMO IN VITRO DE Trichoderma harzianum Rifai SOBRE Fusarium oxysporum Schlecht f. sp passiflorae EN MARACUYÁ (Passiflora edulis Sims var. Flavicarpa DEL MUNICIPIO ZONA BANANERA COLOMBIANA ANTAGONISM IN VITRO OF Trichoderma harzianum Rifai AGAINST Fusarium oxysporum Schlecht f. sp passiflorae IN PASSION FRUIT (Passiflora edulis Sims var. Flavicarpa FROM COLOMBIAN BANANERA ZONE MUNICIPALITY
Reinel José Fernández Barbosa
determining the antagonistic capacity of 6 strains of Trichoderma harzianum against the pathogen. 3 commercial strains were evaluated (TCC-001, TCC-005 and TCC-006 and 3 isolated from soil cultivated with palm oil in the Research Center Caribia of Corpoica (TCN-009, TCN-010, TCN-014. These were evaluated under conditions in vitro using the technique of dual cultivation in Petri plates with Agar Sabouraud. Competition for nutritious and space, micoparasitism and Percentage of Radial Growth Inhibition (PRGI was evaluated, incubating them for 10 days at 28 ºC. A totally randomized design settled down, with 13 treatments and 3 repetitions. All the isolates of T. harzianum exceeded in growth to F. oxysporum with a pathogen growth radiu averages (PGR of 7.42 cm in dual culture. While the pathogen showed average radiu of 1.99 cm. TCN-009 and TCC-006 expressed the best results in competition for nutrients and space to grow 4 times faster than F. oxysporum and to reduce 3 times less the PRGI compared with the control, without significant differences between treatments (P=0.0001; also, produced the largest PRGI to 10 days with values of 64.61 and 65.91% respectively. There was no significant difference when comparing commercial and native isolates, but for the indigenous nature of the isolation, TCN-009 is, an in vitro level, more promising in the search for an antagonist in the control F. oxysporum in similar agroclimatic regions to the Bananera Zone Colombian.
Full Text Available The Type Three Secretion System (T3SS, or injectisome, is a macromolecular infection machinery present in many pathogenic Gram-negative bacteria. It consists of a basal body, anchored in both bacterial membranes, and a hollow needle through which effector proteins are delivered into the target host cell. Two different architectures of the T3SS needle have been previously proposed. First, an atomic model of the Salmonella typhimurium needle was generated from solid-state NMR data. The needle subunit protein, PrgI, comprises a rigid-extended N-terminal segment and a helix-loop-helix motif with the N-terminus located on the outside face of the needle. Second, a model of the Shigella flexneri needle was generated from a high-resolution 7.7-Å cryo-electron microscopy density map. The subunit protein, MxiH, contains an N-terminal α-helix, a loop, another α-helix, a 14-residue-long β-hairpin (Q51-Q64 and a C-terminal α-helix, with the N-terminus facing inward to the lumen of the needle. In the current study, we carried out solid-state NMR measurements of wild-type Shigella flexneri needles polymerized in vitro and identified the following secondary structure elements for MxiH: a rigid-extended N-terminal segment (S2-T11, an α-helix (L12-A38, a loop (E39-P44 and a C-terminal α-helix (Q45-R83. Using immunogold labeling in vitro and in vivo on functional needles, we located the N-terminus of MxiH subunits on the exterior of the assembly, consistent with evolutionary sequence conservation patterns and mutagenesis data. We generated a homology model of Shigella flexneri needles compatible with both experimental data: the MxiH solid-state NMR chemical shifts and the state-of-the-art cryoEM density map. These results corroborate the solid-state NMR structure previously solved for Salmonella typhimurium PrgI needles and establish that Shigella flexneri and Salmonella typhimurium subunit proteins adopt a conserved structure and orientation in their