ArticleParasites & vectors2015
Ascaris lumbricoides β carbonic anhydrase: a potential target enzyme for treatment of ascariasis.
Article in Parasites & vectors, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 32 citations in OpenAlex.
- Synergistic antidiabetic efficacy of dorzolamide and metformin: HPTLC quantification and biological evaluation.Scientific reports · 2026Article
- Sulphonamide inhibition studies of the β-carbonic anhydrase GsaCAβ present in the salmon platyhelminth parasiteJournal of enzyme inhibition and medicinal chemistry · 2023Article
- Cloning, characterization, and inhibition of the novel β-carbonic anhydrase from parasitic blood fluke,Journal of enzyme inhibition and medicinal chemistry · 2023Article
- Genome Study of α-, β-, and γ-Carbonic Anhydrases from the Thermophilic Microbiome of Marine Hydrothermal Vent Ecosystems.Biology · 2023Article
- Cloning, purification, kinetic and anion inhibition studies of a recombinant β-carbonic anhydrase from the Atlantic salmon parasite platyhelminthJournal of enzyme inhibition and medicinal chemistry · 2022Article
- A reverse vaccinology approach on transmembrane carbonic anhydrases from Plasmodium species as vaccine candidates for malaria prevention.Malaria journal · 2022Article
- Emerging trends in environmental and industrial applications of marine carbonic anhydrase: a review.Bioprocess and biosystems engineering · 2022Review
- The Targeting of Noncoding RNAs by Quercetin in Cancer Prevention and Therapy.Oxidative medicine and cellular longevity · 2022Review
- Rapid determination of nematode cell and organ susceptibility to toxic treatments.International journal for parasitology. Drugs and drug resistance · 2020Article
- Biochemical and structural characterisation of a protozoan beta-carbonic anhydrase fromJournal of enzyme inhibition and medicinal chemistry · 2020Article
- Application of System Biology to Explore the Association of Neprilysin, Angiotensin-Converting Enzyme 2 (ACE2), and Carbonic Anhydrase (CA) in Pathogenesis of SARS-CoV-2.Biological procedures online · 2020Article
- Phytochemicals as Modulators of Long Non-Coding RNAs and Inhibitors of Cancer-Related Carbonic Anhydrases.International journal of molecular sciences · 2019Review
- Homology modeling and molecular dynamics dimulation study of β carbonic anhydrase of Ascaris lumbricoides.Bioinformation · 2019Article
- Crystal structure and chemical inhibition of essential schistosome host-interactive virulence factor carbonic anhydrase SmCA.Communications biology · 2019Article
- Involvement of β-Carbonic Anhydrase Genes in Bacterial Genomic Islands and Their Horizontal Transfer to Protists.Applied and environmental microbiology · 2018Article
- Horizontal transfer of β-carbonic anhydrase genes from prokaryotes to protozoans, insects, and nematodes.Parasites & vectors · 2016Article
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundA parasitic roundworm, Ascaris lumbricoides, is the causative agent of ascariasis, with approximately 760 million cases around the world. Helminthic infections occur with a high prevalence mostly in tropical and developing xcountries. Therefore, design of affordable broad-spectrum anti-helminthic agents against a variety of pathogens, including not only A. lumbricoides but also hookworms and whipworms, is desirable. Beta carbonic anhydrases (β-CAs) are considered promising targets of novel anthelminthics because these enzymes are present in various parasites, while completely absent in vertebrates.
methodsIn this study, we identified an A. lumbricoides β-CA (AIBCA) protein from protein sequence data using bioinformatics tools. We used computational biology resources and methods (including InterPro, CATH/Gene3D, KEGG, and METACYC) to analyze AlBCA and define potential roles of this enzyme in biological pathways. The AlBCA gene was cloned into pFastBac1, and recombinant AIBCA was produced in sf-9 insect cells. Kinetics of AlBCA were analyzed by a stopped-flow method.
resultsMultiple sequence alignment revealed that AIBCA contains the two sequence motifs, CXDXR and HXXC, typical for β-CAs. Recombinant AIBCA showed significant CA catalytic activity with kcat of 6.0 × 10(5) s(-1) and kcat/KM of 4.3 × 10(7) M(-1) s(-1). The classical CA inhibitor, acetazolamide, showed an inhibition constant of 84.1 nM. Computational modeling suggests that the molecular architecture of AIBCA is highly similar to several other known β-CA structures. Functional predictions suggest that AIBCA might play a role in bicarbonate-mediated metabolic pathways, such as gluconeogenesis and removal of metabolically produced cyanate.
conclusionsThese results open new avenues to further investigate the precise functions of β-CAs in parasites and suggest that novel β-CA specific inhibitors should be developed and tested against helminthic diseases.
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