A cathepsin L-like protease from Strongylus vulgaris: An orthologue of Caenorhabditis elegans CPL-1

Ultaigh, Sinéad Nic An; Carolan, James C.; Britton, Collette; Murray, Linda; Ryan, M. F.

doi:10.1016/j.exppara.2008.11.002

Cited by 6 publications

(4 citation statements)

References 43 publications

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“…Cathepsins B and B-like proteases are identified in various species 3 . Cathepsins B-like and L-like cysteine proteases are found in Caenorhabditis elegans 4 , 5 . Similar proteases are also detected in some invertebrates 6 .…”

Section: Introductionmentioning

confidence: 99%

Evolutionary History of Cathepsin L (L-like) Family Genes in Vertebrates

Zhou¹,

Zhang

et al. 2015

Int. J. Biol. Sci.

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Cathepsin L family, an important cysteine protease found in lysosomes, is categorized into cathepsins B, F, H, K, L, S, and W in vertebrates. This categorization is based on their sequence alignment and traditional functional classification, but the evolutionary relationship of family members is unclear. This study determined the evolutionary relationship of cathepsin L family genes in vertebrates through phylogenetic construction. Results showed that cathepsins F, H, S and K, and L and V were chronologically diverged. Tandem-repeat duplication was found to occur in the evolutionary history of cathepsin L family. Cathepsin L in zebrafish, cathepsins S and K in xenopus, and cathepsin L in mice and rats underwent evident tandem-repeat events. Positive selection was detected in cathepsin L-like members in mice and rats, and amino acid sites under positive selection pressure were calculated. Most of these sites appeared at the connection of secondary structures, suggesting that the sites may slightly change spatial structure. Severe positive selection was also observed in cathepsin V (L2) of primates, indicating that this enzyme had some special functions. Our work provided a brief evolutionary history of cathepsin L family and differentiated cathepsins S and K from cathepsin L based on vertebrate appearance. Positive selection was the specific cause of differentiation of cathepsin L family genes, confirming that gene function variation after expansion events was related to interactions with the environment and adaptability.

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Section: Introductionmentioning

confidence: 99%

Evolutionary History of Cathepsin L (L-like) Family Genes in Vertebrates

Zhou¹,

Zhang

et al. 2015

Int. J. Biol. Sci.

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“…C. elegans cpl-1 mutant embryos showed decreased cell division rate, arrest of morphogenesis and eventual death, and it was shown that Ce-CPL-1 was involved in the degradation of yolk 32 , 40 , which provides the major nutrients for developing embryos. Transgenic expression of the H. contortus cpl-1 or S. vulgaris cpl-1 genes rescued the embryonic lethal phenotype of the C. elegans cpl-1 mutant, supporting their function in embryonic development 41 , 42 . Here, we show that Dd-cpl-1 RNAi embryos of D. destructor shared similar phenotypes with the C. elegans cpl-1 mutant, such as the dramatically slow cell division, abortive morphogenesis and embryonic lethal phenotype.…”

Section: Discussionmentioning

confidence: 79%

Silencing Ditylenchus destructor cathepsin L-like cysteine protease has negative pleiotropic effect on nematode ontogenesis

Huang,

Cong,

Liu

et al. 2024

Sci Rep

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Ditylenchus destructor is a migratory plant-parasitic nematode that severely harms many agriculturally important crops. The control of this pest is difficult, thus efficient strategies for its management in agricultural production are urgently required. Cathepsin L-like cysteine protease (CPL) is one important protease that has been shown to participate in various physiological and pathological processes. Here we decided to characterize the CPL gene (Dd-cpl-1) from D. destructor. Analysis of Dd-cpl-1 gene showed that Dd-cpl-1 gene contains a signal peptide, an I29 inhibitor domain with ERFNIN and GNFD motifs, and a peptidase C1 domain with four conserved active residues, showing evolutionary conservation with other nematode CPLs. RT-qPCR revealed that Dd-cpl-1 gene displayed high expression in third-stage juveniles (J3s) and female adults. In situ hybridization analysis demonstrated that Dd-cpl-1 was expressed in the digestive system and reproductive organs. Silencing Dd-cpl-1 in 1-cell stage eggs of D. destructor by RNAi resulted in a severely delay in development or even in abortive morphogenesis during embryogenesis. The RNAi-mediated silencing of Dd-cpl-1 in J2s and J3s resulted in a developmental arrest phenotype in J3 stage. In addition, silencing Dd-cpl-1 gene expression in female adults led to a 57.43% decrease in egg production. Finally, Dd-cpl-1 RNAi-treated nematodes showed a significant reduction in host colonization and infection. Overall, our results indicate that Dd-CPL-1 plays multiple roles in D. destructor ontogenesis and could serve as a new potential target for controlling D. destructor.

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“…These were amplified using primers designed to the most conserved regions of the incognita, belongs to a family of proteins that affect a broad range of biological processes, including nutrition, digestion and tissue penetration, and may influence the host-parasite relationship (Neveu et al, 2003;Ultaigh et al, 2009). In plant-parasitic nematodes this enzyme is specifically expressed in the intestinal cells and is associated with food digestion and protein degradation (Hassan et al, 2010;Haegeman et al, 2012).…”

Section: Discussionmentioning

confidence: 99%

“…The expression of the cpl-1 gene occurred equally in eggs, J2 and females of M. hispanica ; however, Shingles et al (2007) reported that in M. incognita the expression of this gene was slightly lower in mature females. The CPL-1 enzyme, identified in secretions of M. incognita , belongs to a family of proteins that affect a broad range of biological processes, including nutrition, digestion and tissue penetration, and may influence the host–parasite relationship (Neveu et al , 2003; Ultaigh et al , 2009). In plant-parasitic nematodes this enzyme is specifically expressed in the intestinal cells and is associated with food digestion and protein degradation (Hassan et al , 2010; Haegeman et al , 2012).…”

Section: Discussionmentioning

confidence: 99%

Molecular characterization of putative parasitism genes in the plant-parasitic nematode Meloidogyne hispanica

et al. 2014

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Meloidogyne hispanica (Mhi) is a difficult-to-control polyphagous root-knot nematode (RKN) species of emerging importance for economically valuable crops. Nematode secretions are likely to be the first signals perceived by the plant and are thought to be involved in various aspects of the plant-nematode interaction. The aims of this work were to identify and characterize M. hispanica parasitism genes: cathepsin L cysteine protease (cpl-1), calreticulin (crt-1), β-1,4-endoglucanase-1 (eng-1) and manganese superoxide dismutase (mnsod). As there are no genomic data available for M. hispanica, primers were designed from the conserved regions of the putative parasitism genes in M. incognita and M. hapla and used to amplify the genes in M. hispanica, which led to the successful amplification of these genes in M. hispanica. Partial gene sequences were also obtained for M. arenaria, M. hapla, M. hispanica, M. incognita and M. javanica cpl-1, crt-1, eng-1 and mnsod genes, and their phylogenetic relationship analysed. In order to determine whether these genes are differentially expressed during M. hispanica development, cDNA was amplified from mRNA isolated from eggs, second-stage juveniles (J2) and females. Amplification products were observed from cDNA of all developmental stages for the Mhi-cpl-1 and Mhi-crt-1 genes. However, the gene Mhi-crt-1 exhibited intense amplification bands in females, while the Mhi-eng-1 gene was equally amplified in eggs and J2 and the Mhi-mnsod gene was only expressed in eggs. In comparison to the other RKN species, the genes Mhi-eng-1 and Mhi-mnsod showed transcription in different nematode developmental stages.

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A cathepsin L-like protease from Strongylus vulgaris: An orthologue of Caenorhabditis elegans CPL-1

Cited by 6 publications

References 43 publications

Evolutionary History of Cathepsin L (L-like) Family Genes in Vertebrates

Evolutionary History of Cathepsin L (L-like) Family Genes in Vertebrates

Silencing Ditylenchus destructor cathepsin L-like cysteine protease has negative pleiotropic effect on nematode ontogenesis

Molecular characterization of putative parasitism genes in the plant-parasitic nematode Meloidogyne hispanica

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