BACKGROUND: Despite the high prevalence of parasitic infections, and their impact on global health and economy, the number of drugs available to treat them is extremely limited. As a result, the potential consequences of large-scale resistance to any existing drugs are a major concern. A number of recent investigations have focused on the effects of potential chemical inhibitors on bacterial and fungal carbonic anhydrases. Among the five classes of carbonic anhydrases (alpha, beta, gamma, delta and zeta), beta carbonic anhydrases have been reported in most species of bacteria, yeasts, algae, plants, and particular invertebrates (nematodes and insects). To date, there has been a lack of knowledge on the expression and molecular structure of beta carbonic anhydrases in metazoan (nematodes and arthropods) and protozoan species. METHODS: Here, the identification of novel beta carbonic anhydrases was based on the presence of the highly-conserved amino acid sequence patterns of the active site. A phylogenetic tree was constructed based on codon-aligned DNA sequences. Subcellular localization prediction for each identified invertebrate beta carbonic anhydrase was performed using the TargetP webserver. RESULTS: We verified a total of 75 beta carbonic anhydrase sequences in metazoan and protozoan species by proteome-wide searches and multiple sequence alignment. Of these, 52 were novel, and contained highly conserved amino acid residues, which are inferred to form the active site in beta carbonic anhydrases. Mitochondrial targeting peptide analysis revealed that 31 enzymes are predicted with mitochondrial localization; one was predicted to be a secretory enzyme, and the other 43 were predicted to have other undefined cellular localizations. CONCLUSIONS: These investigations identified 75 beta carbonic anhydrases in metazoan and protozoan species, and among them there were 52 novel sequences that were not previously annotated as beta carbonic anhydrases. Our results will not only change the current information in proteomics and genomics databases, but will also suggest novel targets for drugs against parasites.
BACKGROUND: Despite the high prevalence of parasitic infections, and their impact on global health and economy, the number of drugs available to treat them is extremely limited. As a result, the potential consequences of large-scale resistance to any existing drugs are a major concern. A number of recent investigations have focused on the effects of potential chemical inhibitors on bacterial and fungal carbonic anhydrases. Among the five classes of carbonic anhydrases (alpha, beta, gamma, delta and zeta), betacarbonic anhydrases have been reported in most species of bacteria, yeasts, algae, plants, and particular invertebrates (nematodes and insects). To date, there has been a lack of knowledge on the expression and molecular structure of betacarbonic anhydrases in metazoan (nematodes and arthropods) and protozoan species. METHODS: Here, the identification of novel betacarbonic anhydrases was based on the presence of the highly-conserved amino acid sequence patterns of the active site. A phylogenetic tree was constructed based on codon-aligned DNA sequences. Subcellular localization prediction for each identified invertebrate betacarbonic anhydrase was performed using the TargetP webserver. RESULTS: We verified a total of 75 betacarbonic anhydrase sequences in metazoan and protozoan species by proteome-wide searches and multiple sequence alignment. Of these, 52 were novel, and contained highly conserved amino acid residues, which are inferred to form the active site in betacarbonic anhydrases. Mitochondrial targeting peptide analysis revealed that 31 enzymes are predicted with mitochondrial localization; one was predicted to be a secretory enzyme, and the other 43 were predicted to have other undefined cellular localizations. CONCLUSIONS: These investigations identified 75 betacarbonic anhydrases in metazoan and protozoan species, and among them there were 52 novel sequences that were not previously annotated as betacarbonic anhydrases. Our results will not only change the current information in proteomics and genomics databases, but will also suggest novel targets for drugs against parasites.
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Authors: M B Guilloton; A F Lamblin; E I Kozliak; M Gerami-Nejad; C Tu; D Silverman; P M Anderson; J A Fuchs Journal: J Bacteriol Date: 1993-03 Impact factor: 3.490
Authors: Sudabeh Iraninasab; Sana Sharifian; Ahmad Homaei; Mozafar Bagherzadeh Homaee; Tanvi Sharma; Ashok Kumar Nadda; John F Kennedy; Muhammad Bilal; Hafiz M N Iqbal Journal: Bioprocess Biosyst Eng Date: 2021-11-25 Impact factor: 3.210
Authors: Reza Zolfaghari Emameh; Harlan R Barker; Martti E E Tolvanen; Seppo Parkkila; Vesa P Hytönen Journal: Parasit Vectors Date: 2016-03-16 Impact factor: 3.876
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Authors: Reza Zolfaghari Emameh; Harlan Barker; Vesa P Hytönen; Martti E E Tolvanen; Seppo Parkkila Journal: Parasit Vectors Date: 2014-08-29 Impact factor: 3.876