scholarly journals Corrigendum to “Interaction between Gallotannin and a Recombinant Form of Arginine Kinase of Trypanosoma brucei: Thermodynamic and Spectrofluorimetric Evaluation”

2018 ◽  
Vol 2018 ◽  
pp. 1-1
Author(s):  
O. S. Adeyemi ◽  
A. F. Sulaiman ◽  
O. M. Iniaghe
Keyword(s):  
Trypanosoma Brucei ◽  
Arginine Kinase ◽  
Recombinant Form

scholarly journals Interaction between Gallotannin and a Recombinant Form of Arginine Kinase of Trypanosoma brucei: Thermodynamic and Spectrofluorimetric Evaluation

2014 ◽  
Vol 2014 ◽  
pp. 1-7 ◽  
Author(s):  
O. S. Adeyemi ◽  
A. F. Sulaiman ◽  
O. M. Iniaghe
Keyword(s):  
Enzyme Activity ◽  
Molecular Docking ◽  
Trypanosoma Brucei ◽  
Arginine Kinase ◽  
Docking Studies ◽  
Recombinant Form ◽  
Binding Properties ◽  
Mechanism Of Inhibition ◽  
Static Data ◽  
Inhibitory Interactions

Current chemotherapies against trypanosomiasis are beset with diverse challenges, a situation which underscores the numerous research efforts aimed at finding newer and effective treatments. Arginine kinase of trypanosome has been validated as target for drug development against trypanosomiasis. The present study investigated the interaction between a recombinant form of the arginine kinase (rTbAK) of trypanosome and gallotannin. The interaction between gallotannin and recombinant arginine kinase of Trypanosoma brucei caused significant decrease of enzyme activity. Kinetic analysis revealed the interaction to be of noncompetitive inhibition. Further thermodynamic analysis showed that the interaction between gallotannin and the recombinant arginine kinase was nonspontaneous and involved hydrophobic forces. The Ksv values and the FRET analysis suggest that static quenching of fluorescence intensity by gallotannin was static. Data revealed inhibitory interactions between gallotannin and rTbAK of trypanosome. Although the mechanism of inhibition is not clear yet, molecular docking studies are ongoing to clearly define the inhibitory interactions between the gallotannin and rTbAK. The knowledge of such binding properties would enrich development of selective inhibitors for the arginine kinase of Trypanosoma brucei.

scholarly journals Flagellar targeting of an arginine kinase requires a conserved lipidated protein intraflagellar transport (LIFT) pathway in Trypanosoma brucei

2020 ◽  
Vol 295 (32) ◽  
pp. 11326-11336
Author(s):  
Maneesha Pandey ◽  
Yameng Huang ◽  
Teck Kwang Lim ◽  
Qingsong Lin ◽  
Cynthia Y. He
Keyword(s):  
Trypanosoma Brucei ◽  
Protein Transport ◽  
Arginine Kinase ◽  
Intraflagellar Transport ◽  
Small Gtpases ◽  
Functional Specialization ◽  
Dependent Manner ◽  
Protozoan Parasites ◽  
Binding Partners ◽  
Sensory Functions

Both intraflagellar transport (IFT) and lipidated protein intraflagellar transport (LIFT) pathways are essential for cilia/flagella biogenesis, motility, and sensory functions. In the LIFT pathway, lipidated cargoes are transported into the cilia through the coordinated actions of cargo carrier proteins such as Unc119 or PDE6δ, as well as small GTPases Arl13b and Arl3 in the cilium. Our previous studies have revealed a single Arl13b ortholog in the evolutionarily divergent Trypanosoma brucei, the causative agent of African sleeping sickness. TbArl13 catalyzes two TbArl3 homologs, TbArl3A and TbArl3C, suggesting the presence of a conserved LIFT pathway in these protozoan parasites. Only a single homolog to the cargo carrier protein Unc119 has been identified in T. brucei genome, but its function in lipidated protein transport has not been characterized. In this study, we exploited the proximity-based biotinylation approach to identify binding partners of TbUnc119. We showed that TbUnc119 binds to a flagellar arginine kinase TbAK3 in a myristoylation-dependent manner and is responsible for its targeting to and enrichment in the flagellum. Interestingly, only TbArl3A, but not TbArl3C interacted with TbUnc119 in a GTP-dependent manner, suggesting functional specialization of Arl3-GTPases in T. brucei. These results establish the function of TbUnc119 as a myristoylated cargo carrier and support the presence of a conserved LIFT pathway in T. brucei.

scholarly journals Apoferritin and Apoferritin-Capped Metal Nanoparticles Inhibit Arginine Kinase of Trypanosoma brucei

Molecules ◽  
2020 ◽  
Vol 25 (15) ◽  
pp. 3432
Author(s):  
Oluyomi Stephen Adeyemi ◽  
Afolake T. Arowolo ◽  
Helal F. Hetta ◽  
Salim Al-Rejaie ◽  
Damilare Rotimi ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Metal Nanoparticles ◽  
Kinetic Parameters ◽  
Trypanosoma Brucei ◽  
Kinase Activity ◽  
Arginine Kinase ◽  
Inhibition Constant ◽  
Binding Properties ◽  
Inhibitory Potential ◽  
Relative Inhibition

The aim of this study was to explore the inhibitory potential of apoferritin or apoferritin-capped metal nanoparticles (silver, gold and platinum) against Trypanosomabrucei arginine kinase. The arginine kinase activity was determined in the presence and absence of apoferritin or apoferritin-capped metal nanoparticles. In addition, kinetic parameters and relative inhibition of enzyme activity were estimated. Apoferritin or apoferritin-capped metal nanoparticles’ interaction with arginine kinase of T. brucei led to a >70% reduction in the enzyme activity. Further analysis to determine kinetic parameters suggests a mixed inhibition by apoferritin or apoferritin-nanoparticles, with a decrease in Vmax. Furthermore, the Km of the enzyme increased for both ATP and L-arginine substrates. Meantime, the inhibition constant (Ki) values for the apoferritin and apoferritin-nanoparticle interaction were in the submicromolar concentration ranging between 0.062 to 0.168 nM and 0.001 to 0.057 nM, respectively, for both substrates (i.e., L-arginine and ATP). Further kinetic analyses are warranted to aid the development of these nanoparticles as selective therapeutics. Also, more studies are required to elucidate the binding properties of these nanoparticles to arginine kinase of T. brucei.

scholarly journals The Flagellar Arginine Kinase in Trypanosoma brucei Is Important for Infection in Tsetse Flies

PLoS ONE ◽  
2015 ◽  
Vol 10 (7) ◽  
pp. e0133676 ◽  
Author(s):  
Cher-Pheng Ooi ◽  
Brice Rotureau ◽  
Simonetta Gribaldo ◽  
Christina Georgikou ◽  
Daria Julkowska ◽  
...  
Keyword(s):  
Trypanosoma Brucei ◽  
Arginine Kinase ◽  
Tsetse Flies

scholarly journals The Phosphoarginine Energy-Buffering System of Trypanosoma brucei Involves Multiple Arginine Kinase Isoforms with Different Subcellular Locations

PLoS ONE ◽  
2013 ◽  
Vol 8 (6) ◽  
pp. e65908 ◽  
Author(s):  
Frank Voncken ◽  
Fei Gao ◽  
Cath Wadforth ◽  
Maggie Harley ◽  
Claudia Colasante
Keyword(s):  
Trypanosoma Brucei ◽  
Arginine Kinase

scholarly journals Flagellar targeting of an arginine kinase requires a conserved lipidated intraflagellar transport (LIFT) pathway in Trypanosoma brucei

2020 ◽  
Author(s):  
Maneesha Pandey ◽  
Yameng Huang ◽  
Teck Kwang Lim ◽  
Qingsong Lin ◽  
Cynthia Y. He
Keyword(s):  
Trypanosoma Brucei ◽  
Protein Transport ◽  
Arginine Kinase ◽  
Intraflagellar Transport ◽  
Small Gtpases ◽  
Functional Specialization ◽  
Dependent Manner ◽  
Protozoan Parasites ◽  
Binding Partners ◽  
Sensory Functions

AbstractBoth intraflagellar transport (IFT) and lipidated intraflagellar transport (LIFT) pathways are essential for cilia/flagella biogenesis, motility and sensory functions. In the LIFT pathway, lipidated cargoes are transported into the cilia through the coordinated actions of cargo carrier proteins such as Unc119 or PDE6δ, as well as small GTPases Arl13b and Arl3 in the cilium. Our previous studies revealed a single Arl13b ortholog in the evolutionarily divergent Trypanosoma brucei. TbArl13 catalyses two TbArl3 homologs, TbArl3A and TbArl3C, suggesting the presence of a conserved LIFT pathway in these protozoan parasites. Only a single homolog to the cargo carrier protein Unc119 was identified in T. brucei genome, but its function in lipidated protein transport has not been characterized. In this study, we exploited the proximity-based biotinylation approach to identify binding partners of TbUnc119. We showed that TbUnc119 binds to a flagellar arginine kinase TbAK3 in a myristoylation-dependent manner and is responsible for its targeting and enrichment in the flagellum. Interestingly, only TbArl3A, but not TbArl3C interacts with TbUnc119 in a GTP-dependant manner, suggesting functional specialization of Arl3-GTPases in T. brucei. This study establishes the function of TbUnc119 as a myristoylated cargo carrier and supports the presence of a conserved LIFT pathway in T. brucei.

Screening of some Asteraceae to discover new active compounds against Trypanosoma brucei by metabolite profiling and PLS analysis

Planta Medica ◽  
2013 ◽  
Vol 79 (13) ◽  
Author(s):  
MS Nogueira ◽  
FB da Costa ◽  
MA Magenta ◽  
M Kaiser ◽  
R Brun ◽  
...  
Keyword(s):  
Trypanosoma Brucei ◽  
Metabolite Profiling ◽  
Active Compounds ◽  
Pls Analysis
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