Publications by authors named "Blanca R Jarilla"
Rabies is a fatal zoonotic disease endemic in developing countries of Asia and Africa. Recently, the direct rapid immunohistochemical test (DRIT) was recommended by the World Health Organization (WHO) and the World Organization for Animal Health (OIE) as a diagnostic test for rabies. Therefore, a biotinylated polyclonal antibody (pAb) against the rabies lyssavirus (RABV) nucleoprotein was developed using a plasmid cDNA vaccine derived from a challenge virus standard 11 strain.
View Article and Find Full Text PDFBackground: Paragonimiasis is a foodborne parasitic infection caused by lung flukes of the genus Paragonimus. Several species of Paragonimus are endemic in Japan: P. westermani (diploid and triploid) P.
View Article and Find Full Text PDFArticle Synopsis
- Phosphagen kinases (PKs) like creatine kinase and taurocyamine kinase (TK) are crucial for energy metabolism in animals, with TK being studied in the trematode Schistosoma japonicum.
- Mutations in specific domains of the SjTK, resulting from site-directed mutagenesis, completely inhibited activity for its substrate taurocyamine, indicating the essential roles of both domains (D1 and D2) in enzymatic function.
- The study further identifies critical amino acid residues in the guanidino specificity region of SjTKD1 that are important for substrate binding, particularly mutations at position R63 that lead to loss of activity.
Article Synopsis
- This research focuses on Clonorchis sinensis, a helminthic parasite that affects the bile duct and is prevalent in East Asia, emphasizing the potential of phosphagen kinases (PK) as drug targets due to their uniqueness in invertebrates.
- A cDNA clone encoding a 717-amino acid polypeptide homologous to taurocyamine kinase was identified, revealing insights into its evolutionary origins and distinct absence in mammalian hosts.
- CsTK exhibits enzymatic activity specific to taurocyamine and is consistently expressed in both adult and developmental stages of C. sinensis, making it a promising candidate for future therapeutic interventions.
Article Synopsis
- The study investigates the unique substrate binding mechanism of the taurocyamine kinase (TK) from Paragonimus westermani through site-directed mutagenesis.
- Mutations at specific amino acid positions (Y84, Y87, and A59) in both domains of TK severely affect its ability to bind and catalyze the substrate taurocyamine.
- Substituting these residues with others (like R, H, and I) leads to significant decreases in enzyme activity, highlighting their importance in substrate recognition and binding.
Article Synopsis
- Taurocyamine kinase (TK) is an enzyme that transfers a phosphate between ATP and taurocyamine, with origins linked to creatine kinase (CK) ancestors in annelids.
- The TK from the lung fluke Paragonimus westermani represents a distinct evolutionary lineage, having evolved from a molluscan arginine kinase (AK) gene.
- The study suggests that exon shuffling played a significant role in altering the amino acid sequence and affinity of the enzyme, enhancing understanding of phosphagen kinase evolution in trematodes.
Article Synopsis
- Phosphagen kinases (PKs), essential for energy metabolism, are present as Creatine kinase (CK) in vertebrates and multiple forms in invertebrates, like Schistosoma japonicum (Sj).
- SjPK displays unique structural features with two functional domains (D1 and D2), each contributing differently to its activity—D1 has a high turnover rate while D2 shows a strong affinity for the substrate taurocyamine.
- These findings suggest SjPK could be a promising target for antihelminthic drugs, as it is specific to parasites and plays a key role in their energy metabolism.
Phosphagen kinases of parasites: unexplored chemotherapeutic targets.
Korean J Parasitol
December 2010
Due to the possible emergence of resistance and safety concerns on certain treatments, development of new drugs against parasites is essential for the effective control and subsequent eradication of parasitic infections. Several drug targets have been identified which are either genes or proteins essential for the parasite survival and distinct from the hosts. These include the phosphagen kinases (PKs) which are enzymes that play a key role in maintenance of homeostasis in cells exhibiting high or variable rates of energy turnover by catalizing the reversible transfer of a phosphate between ATP and naturally occurring guanidine compounds.
View Article and Find Full Text PDFArticle Synopsis
- The study reveals that taurocyamine kinase (TK), previously believed to be specific to certain marine annelids, is also found in the lung fluke Paragonimus westermani.
- P. westermani's TK has a unique structure with two domains, sharing similarities to molluscan arginine kinase and showing strong activity for taurocyamine, enhancing substrate binding.
- Targeting P. westermani TK with inhibitors could lead to new treatments for infections and aid in the development of diagnostic methods for paragonimiasis.