Fascioliasis, a neglected foodborne disease caused by liver flukes
(genus Fasciola), affects more than 200 million people
worldwide. Despite technological advances, little is known about the
molecular biology and biochemistry of these flukes. We present the
draft genome of Fasciola gigantica for
the first time. The assembled draft genome has a size of ∼1.04
Gb with an N50 and N90 of 129 and 149 kb, respectively. A total of
20 858 genes were predicted. The de novo repeats
identified in the draft genome were 46.85%. The pathway included all
of the genes of glycolysis, Krebs cycle, and fatty acid metabolism
but lacked the key genes of the fatty acid biosynthesis pathway. This
indicates that the fatty acid required for survival of the fluke may
be acquired from the host bile. It may be hypothesized that the relatively
larger F. gigantica genome did not
evolve through genome duplications but rather is interspersed with
many repetitive elements. The genomic information will provide a comprehensive
resource to facilitate the development of novel interventions for
fascioliasis control.
A solitary bone cyst is a non-neoplastic osseous lesion comprising 1% of all the cysts affecting the jaws. They are generally asymptomatic, usually detected incidentally during routine radiological assessment and are less common in the mandibular anterior region. This article presents a well-documented case involving a solitary bone cyst affecting the mandibular symphysis in a 12-year-old boy with no history of previous trauma. Simple curettage of the bone cavity resulted in the resolution of the lesion with progressive osseous regeneration. No evidence of recurrence was noted 2 years after the treatment.
The asparaginyl-tRNA synthetase (NRS) catalyzes the attachment of asparagine to its cognate tRNA during translation. NRS first catalyzes the binding of Asn and ATP to form the NRS-asparaginyl adenylate complex, followed by the esterification of Asn to its tRNA. We investigated the role of constituent domains in regulating the structure and activity of Fasciola gigantica NRS (FgNRS). We cloned the full-length FgNRS, along with its various truncated forms, expressed, and purified the corresponding proteins. Size exclusion chromatography indicated a role of the anticodon-binding domain (ABD) of FgNRS in protein dimerization. The N-terminal domain (NTD) was not essential for cognate tRNA binding, and the hinge region between the ABD and the C-terminal domain (CTD) was crucial for regulating the enzymatic activity. Molecular docking and fluorescence quenching experiments elucidated the binding affinities of the substrates to various domains. The molecular dynamics simulation of the modeled protein showed the presence of an unstructured region between the NTD and ABD that exhibited a large number of conformations over time, and further analysis indicated this region to be intrinsically disordered. The present study provides information on the structural and functional regulation, protein-substrate(s) interactions and dynamics, and the role of non-catalytic domains in regulating the activity of FgNRS.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.