Fasciola hepatica leucine aminopeptidase, a promising candidate for vaccination against ruminant fasciolosis☆

Acosta, Daniel; Cancela, Mario; Piacenza, Lucı́a; Roche, Leda; Carmona, Carlos; Tort, José F.

doi:10.1016/j.molbiopara.2007.11.011

Cited by 84 publications

(51 citation statements)

References 54 publications

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“…(Gropp et al 2009) or affect inflammatory responses (Naglik et al 2003). Indeed, immunization with leucine aminopeptidase shows high level of protection with Fasciola hepatica demonstrating its efficacy as a vaccine candidate (Acosta et al 2008). Enzymes belonging to the cytosolic protein degradation pathway consisting of ATP-dependent proteases and ATP-independent peptidases are also known to play important roles in modulating the host response.…”

Section: Introductionmentioning

confidence: 99%

Roles of Salmonella enterica serovar Typhimurium encoded Peptidase N during systemic infection of Ifnγ−/− mice

2012

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Section: Introductionmentioning

confidence: 99%

Roles of Salmonella enterica serovar Typhimurium encoded Peptidase N during systemic infection of Ifnγ−/− mice

2012

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“…3) have been utilized as synthetic fluorogenic and highly specific substrates for aminopeptidases, in which case hydrolysis of the amide bond results in liberation of the fluorescent AMC (Iwaki et al, 1986;Acosta et al, 2008;Budič et al, 2009;Semashko et al, 2008;Chung, 2008;Townsend, 2009). As a result, such substrates offer rapid detection, visualization and assay of various aminopeptidase enzymes from different / target microorganisms in samples or plant extracts (Iwaki et al, 1986;Acosta et al, 2008;Budič et al, 2009;Semashko et al, 2008;Chung, 2008;Townsend, 2009).…”

Section: Introductionmentioning

confidence: 99%

Synthesis and Fluorogenic Properties of Some 1-(Coumarin-7-yl)-4,5-dihydro-1,2,4-triazin-6(1H)-ones

Mustafa¹,

El‐Abadelah²,

Mubarak³

et al. 2011

IJC

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Herein, we have synthesized and tested a selected set of N1-(coumarin-7-yl)-4,5-dihydro-1,2,4-triazin-6(1H)-ones (8) incorporating masked α-amino acids within the triazinone skeleton as synthetic fluorogenic substrates for amino peptidases using human nasal epithelium that expressed aminopeptidases. These chiral triazinones, obtained via direct interaction of α-amino esters with N1-(coumarin-7-yl) nitrile imine (generated in situ from its hydrazonoyl chloride by the action of triethylamine), bear close resemblance to 7-amino-4-methylcoumarin (AMC) with labeled α-amino acids (AA-AMC's/7). The aminopeptidase activity of the synthesized compounds (0.125 and 0.5 mM) was compared with that of a model compound L-alanine-4-methylcoumaryl-7-amide (Ala-MCA), following in-house validation of the aminopeptidase activities of the human nasal primary culture. In comparison to the model aminopeptidase substrate (Ala-MCA), the synthesized compounds yielded fluorescent 7-amino-4-methylcoumarin following incubation with nasal epithelial cells. However, the yield was significantly lower than was observed for the control compound.

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“…Several F. hepatica recombinant antigens have been purified to enhance the specificity of the diagnostic assays (8,15,32,62). Some of these antigens have also been found to be excellent immunogens capable of inducing partial protection against a challenge F. hepatica infection in a variety of experimental models (1,3,9,21,28). Most notable are fatty acid binding proteins (FABPs) (36), cathepsin proteases (60), and saposin like-proteins (FhSAP2) (32), which have been documented as useful immunodiagnostic molecules for fascioliasis.…”

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confidence: 99%

Biochemical Characterization and Differential Expression of a 16.5-Kilodalton Tegument-Associated Antigen from the Liver Fluke Fasciola hepatica

Gaudier

Cabán-Hernández

Osuna

et al. 2012

Clin. Vaccine Immunol.

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ABSTRACTA cDNA encoding a 16.5-kDa protein termed FhTP16.5 was identified by immunoscreening of a cDNA library fromFasciola hepaticaadult flukes using pooled sera from rabbits infected withF. hepaticafor 4 weeks. Quantitative reverse transcriptase PCR (qPCR) analysis revealed that FhTP16.5 is not expressed in unembryonated eggs. It is poorly expressed in miracidia and highly expressed at the juvenile and adult stages; however, significant differences were found between the expression levels of FhTP16.5 in juveniles versus adult flukes. Recombinant FhTP16.5 was expressed at high levels inEscherichia coli, purified by affinity chromatography, and used to raise anti-FhTP16.5 polyclonal antibodies in rabbits. Immunoblot analysis using the anti-FhTP16.5 IgG antibody identified FhTP16.5 in crude and tegumental extracts and in excretory-secretory products ofF. hepatica. The protein was not detected in crude extracts ofSchistosoma mansoniorSchistosomajaponicum. Antibodies to FhTP16.5 were detected in the sera of rabbits at 3 to 12 weeks ofF. hepaticainfection as well as in the sera of humans with chronic fascioliasis; these findings suggest that FhTP16.5 could be a good antigen for serodiagnosis of fascioliasis. Immunohistochemistry demonstrated that FhTP16.5 localizes to the surface of the tegument of various developmental stages and in parenchymal tissues of the adult fluke. Such specific localization makes FhTP16.5 an attractive target for immunoprophylaxis or chemotherapy.

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Fasciola hepatica leucine aminopeptidase, a promising candidate for vaccination against ruminant fasciolosis☆

Cited by 84 publications

References 54 publications

Roles of Salmonella enterica serovar Typhimurium encoded Peptidase N during systemic infection of Ifnγ−/− mice

Roles of Salmonella enterica serovar Typhimurium encoded Peptidase N during systemic infection of Ifnγ−/− mice

Synthesis and Fluorogenic Properties of Some 1-(Coumarin-7-yl)-4,5-dihydro-1,2,4-triazin-6(1H)-ones

Biochemical Characterization and Differential Expression of a 16.5-Kilodalton Tegument-Associated Antigen from the Liver Fluke Fasciola hepatica

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