Phylogeny of Antigen‐Processing Enzymes: Cathepsins of a Cephalochordate, an Agnathan and a Bony Fish

Uinuk-ool, Tatiana S.; Takezaki, Naoko; Kuroda, Noriyuki; Figueroa, Felipe; Sato, Akie; Samonte, Irene E.; Mayer, Werner E.; Klein, Jörg

doi:10.1046/j.1365-3083.2003.01322.x

Cited by 41 publications

(29 citation statements)

References 71 publications

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“…The remaining trees were combined to find the maximum a posteriori probability estimate of the phylogeny. The topology of the resulting trees was rooted according to results obtained by several studies that provided structural and phylogenetic evidence for the existence of two distinct subfamilies, the L-like and the B-like subfamilies, distinguished by the presence and absence of the ERFNIN motif, respectively (Karrer et al 1993;Berti and Storer 1995;Uinuk-ool et al 2003).…”

Section: Phylogenetic Analysis Of Cathepsins and Silicateinsmentioning

confidence: 99%

“…The molecular evolution of cathepsins B, H, and L has been explored in a handful of animals, predominantly vertebrates (Uinuk-ool et al 2003). However, few invertebrate taxa were represented in that study, hampering a reliable inference of the relationships among the specific cathepsins from different animal phyla and, reciprocally, Nosenko et al (2013) and appearance of silicatein (black dot).…”

Section: Introductionmentioning

confidence: 99%

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A Proposal for the Evolution of Cathepsin and Silicatein in Sponges

et al. 2015

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Cathepsins are enzymes capable of degrading proteins intracellularly. They occur ubiquitously in opisthokonts, but their potential to provide insight across the evolutionary transition from protists to metazoans remains poorly investigated. Here, we explore the evolution of cathepsins using comparative analyses of transcriptomic datasets, focusing on both, protists (closely related to metazoans), and early divergent animals (i.e., sponges). We retrieved DNA sequences of nine cathepsin types (B, C, D, F, H, L, O, Z, and silicatein) in the surveyed taxa. In choanoflagellates, only five types (B, C, L, O, Z) were identified, all of them being also found in sponges, indicating that while all cathepsins present in protists were conserved across metazoan lineages, cathepsins F and H (and probably D) are metazoan acquisitions. The phylogeny of cysteine protease cathepsins (excluding cathepsin D) revealed two major lineages: lineage B (cathepsins B and C) and lineage L (cathepsins F, H, L, O, Z). In the latter lineage, a mutation at the active site of cathepsin L gave rise to silicatein, an enzyme exclusively known to date from siliceous sponges and involved in the production of their silica spicules. However, we found that several sponges with siliceous spicules did not express silicatein genes and that, in contrast, several aspiculate sponges did contain silicatein genes. Our results suggest that the ability to silicify may have evolved independently within sponges, some of them losing this capacity secondarily. We also show that most phylogenies based on cathepsin and silicatein genes (except for that of cathepsin O) failed to recover the major lineages of sponges.

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Section: Phylogenetic Analysis Of Cathepsins and Silicateinsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

A Proposal for the Evolution of Cathepsin and Silicatein in Sponges

et al. 2015

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“…The evolutionary history of CsCath B was inferred using the Neighbor-Joining method on MEGA 5. The evolutionary distances were computed using the Poisson correction method (Uinuk-Ool et al, 2003). The 3D structure of the CsCath B protein was predicted by utilizing the I-Tasser server (http://zhanglab.ccmb.med.umich.edu/I-TASSER).…”

Section: Cdna Library Construction Identification and Bioinformaticsmentioning

confidence: 99%

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Arockiaraj¹,

Kumaresan²,

Chaurasia³

et al. 2014

Turk. J. Fish. Aquat. Sci.

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In this study, we have reported a full length cDNA of cathepsin B identified from the constructed cDNA library of snakehead murrel Channa striatus by genome sequence FLX technology. . CsCath B exhibited the maximum similarity (87%) with Cath B from mangrove red snapper, Lutjanus argentimaculatus. Phylogenetically, CsCath B is clustered together with the fish groups belonging to perciformes. A predicted 3D model of CsCath B revealed 11 α-helix and 10 β-strands. CsCath B contains higher percentage (10%) of coils due to the presence of many glycine residues (36 residues). The highest gene expression (P<0.05) was noticed in liver. Further, the expression was induced with fungal (Aphanomyces invadans) and bacterial (Aeromonas hydrophila) infections. The predicted antimicrobial region of CsCath B was synthesized to study its antimicrobial property. The peptide exhibited the antimicrobial activity towards Gram negative and Gram positive bacteria. The overall results indicate that CsCath B is a potential molecule for further studies on murrel defense mechanism.

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“…The evolutionary history of CsCath L was inferred using the neighbour-joining method. The evolutionary distances were computed using the Poisson correction method (Uinuk-Ool et al 2003). The phylogenetic analysis involved 30 amino acid sequences including CsCath L. The phylogenetic tree was conducted in MEGA 5 (Tamura et al 2011).…”

Section: Bioinformatics Characterization Of Cscath Lmentioning

confidence: 99%

“…Cathepsins are enzymes that have been cleaving peptide bonds of lysosomal proteins probably since lysosomes appeared in early eukaryotes. When the adaptive system emerged in gnathostomes, cathepsins evolved to produce peptides in the major histocompatibility complex class II molecules (Uinuk-Ool et al 2003). During the past few years, many of the cathepsins have been accredited with more specific functions in human, including bone re-modelling, antigen presentation, epidermal homeostasis, pro-hormone processing, maintenance of the central nervous system, angiogenesis, cell death and cancer cell invasion (Reinheckel et al 2001;Turk et al 2001;Balaji et al 2002;Felbor et al 2002).…”

Section: Introductionmentioning

confidence: 99%

A murrel cysteine protease, cathepsin L: bioinformatics characterization, gene expression and proteolytic activity

et al. 2014

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Cathepsin L, a lysosomal endopeptidase, is a member of the peptidase C1 family (papain-like family) of cysteine proteinases that cleave peptide bonds of lysosomal proteins. In this study, we report a cathepsin L sequence identified from the constructed cDNA library of striped murrel Channa striatus (designated as CsCath L) using genome sequencing FLX TM technology. The full-length CsCath L contains three eukaryotic thiol protease domains at positions 134-145, 278-288 and 299-318. Phylogenetic analysis revealed that the CsCath L was clustered together with other cathepsin L from teleosts. The three-dimensional structure of CsCath L modelled by the I-Tasser program was compared with structures deposited in the Protein Data Bank to find out the structural similarity of CsCath L with experimentally identified structures. The results showed that the CsCath L exhibits maximum structural identity with pro-cathepsin L from human. The RNA fold structure of CsCath L was predicted along with its minimum free energy (-471.93 kcal/mol). The highest CsCath L gene expression was observed in liver, which was also significantly higher (P < 0.05) than that detected in other tissues taken for analysis. In order to investigate the mRNA transcription profile of CsCath L during infection, C. striatus were injected with fungus (Aphanomyces invadans) and bacteria (Aeromonas hydrophila) and its expression was up-regulated in liver at various time points. Similar to gene expression studies, the highest CsCath L enzyme activity was also observed in liver and its activity was up-regulated by fungal and bacterial infections.

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Phylogeny of Antigen‐Processing Enzymes: Cathepsins of a Cephalochordate, an Agnathan and a Bony Fish

Cited by 41 publications

References 71 publications

A Proposal for the Evolution of Cathepsin and Silicatein in Sponges

A Proposal for the Evolution of Cathepsin and Silicatein in Sponges

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A murrel cysteine protease, cathepsin L: bioinformatics characterization, gene expression and proteolytic activity

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