Cathepsin B-like and hemoglobin-type cysteine proteases: Stage-specific gene expression in Angiostrongy cantonensis

Ni, Fang; Wang, Yinan; Zhang, Jing; Yu, Long-Chuan; Fang, Wenzhen; Luo, Damin

doi:10.1016/j.exppara.2012.05.014

Cited by 12 publications

(16 citation statements)

References 33 publications

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“…Obviously, consistent with the infective stage of L3 is an intense staining of AC-cathBs in the esophagus and excretory. So, the results in this report further supported our previous observations resulting from Signal-P, RT-PCR, and western blot analyses (Fang et al, 2010;Ni et al, 2012), and from electrospray ionization mass spectrometry (Morassutti et al, 2012). There is a big difference in the structure between larvae and adults, no lateral glands and lateral alae could be seen in the body wall of adult A. cantonensis, while they were more obvious in L1 and L3 (Xu et al, 1989;Ding et al, 1990).…”

Section: Discussionsupporting

confidence: 95%

“…for cathepsin B-like cysteine protease genes 1, 2 (AC-cathB-1, AC-cathB-2) of A. cantonensis (Ni et al, 2012). Forward primer MEcathB-1F (5 0 -CGGGGTACCTCAGA AGACAACGACAAT-3 0 ) and reverse primer (MEcathB-1R 5 0 -ACGC GTCGACACAGACAATGAAGTGGAA-3 0 ) for AC-cathB-1 (HQ110099); Forward primer MEcathB-2F (5 0 -CGGGGTACCGTCTCGGCAG-CATCTTGGC-3 0 ) and reverse primer (MEcathB-2R 5 0 -ACGCGTC-GACATTTCGGTTCTCCGGCAA-3 0 ) for AC-cathB-2 (HQ110100) with restriction enzyme of Kpn I and Sal I (underlined), respectively.…”

Section: Rna Extraction and Reverse Transcriptionmentioning

confidence: 99%

“…Haematophagous nematodes express proteases of different mechanistic classes in their intestines, many of which have proven or putative roles in degradation of haemoglobin and other proteins involved in nutrition, however, most of the proteases described previously are expressed in the intestine and many of them do not appear in excretory/ secretory (ES) products, implying that they act locally in the intestine (Williamson et al, 2003). The ES products and the characterization of cathepsin B protease in different stages of development in Angiostrongylus cantonensis has been described using Signal-P (Fang et al, 2010), RT-PCR, and western blot analyses (Ni et al, 2012), however, there are no data that directly support the cathepsin B protease (AC-cathB-1, -2) were released by the parasite as ES products and the anatomic location of the proteases in A. cantonensis remains unclear. Here we look at the anatomical localization and expression characterization of two cysteine proteases (ACcathB-1, -2) in order to assist us in understanding better the role of cathepsin B in the A. cantonensis.…”

Section: Introductionmentioning

confidence: 97%

See 2 more Smart Citations

Immunolocalization and developmental expression patterns of two cathepsin B proteases (AC-cathB-1, -2) of Angiostrongylus cantonensis

Yu¹,

Wang²,

Zhang³

et al. 2014

Experimental Parasitology

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Section: Discussionsupporting

confidence: 95%

Section: Rna Extraction and Reverse Transcriptionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 97%

See 1 more Smart Citation

Immunolocalization and developmental expression patterns of two cathepsin B proteases (AC-cathB-1, -2) of Angiostrongylus cantonensis

Yu¹,

Wang²,

Zhang³

et al. 2014

Experimental Parasitology

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“…RT-PCR and quantitative real-time RT-PCR enabled identification of two genes expressed in a stage-specific manner ( AC-cathB-1 , AC-cathB-2 ) in Angiostrongylus cantonensis (Chen). AC-cathB-1 and AC-cathB-2 were expressed in L1 and L3, respectively, suggesting that AC-cathB-1 and AC-cathB-2 may play an important role in intermediate and final host invasion [32]. …”

Section: Resultsmentioning

confidence: 99%

Screening and Functional Analysis of the Peroxiredoxin Specifically Expressed in Bursaphelenchus xylophilus—The Causative Agent of Pine Wilt Disease

Ren

Huang

et al. 2014

IJMS

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The pine wood nematode, Bursaphelenchus xylophilus, is the causal agent of pine wilt disease. Accurately differentiating B. xylophilus from other nematodes species, especially its related species B. mucronatus, is important for pine wood nematode detection. Thus, we attempted to identify a specific protein in the pine wood nematode using proteomics technology. Here, we compared the proteomes of B. xylophilus and B. mucronatus using Two-dimensional gel electrophoresis (2-DE) and matrix-assisted laser desorption/ionization-time-of-flight/time-of-flight (MALDI-TOF/TOF-MS) technologies. In total, 15 highly expressed proteins were identified in B. xylophilus compared with B. mucronatus. Subsequently, the specificity of the proteins identified was confirmed by PCR using the genomic DNA of other nematode species. Finally, a gene encoding a specific protein (Bx-Prx) was obtained. This gene was cloned and expressed in E. coli. The in situ hybridisation pattern of Bx-Prx showed that it was expressed strongly in the tail of B. xylophilus. RNAi was used to assess the function of Bx-Prx, the results indicated that the gene was associated with the reproduction and pathogenicity of B. xylophilus. This discovery provides fundamental information for identifying B. xylophilus via a molecular approach. Moreover, the purified recombinant protein has potential as a candidate diagnostic antigen of pine wilt disease, which may lead to a new immunological detection method for the pine wood nematode.

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“…They are cathepsin B-like enzyme gene, 1, 2 (AC-cathB-1, AC-cathB-2), and hemoglobin-type cysteine protease gene (AC-hem) (Fang et al 2010). A cysteine protease gene has also been isolated and described from the adult worm (Ni et al 2012). Cysteine protease is a potential new target for the development of novel antimalarial drugs.…”

Section: Discussionmentioning

confidence: 99%

Transcriptome profiling of the fifth-stage larvae of Angiostrongylus cantonensis by next-generation sequencing

et al. 2013

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Angiostrongylus cantonensis is an important zoonotic nematode. It is the causative agent of eosinophilic meningitis and eosinophilic meningoencephalitis in humans. However, information of this parasite at the genomic level is very limited. In the present study, the transcriptomic profiles of the fifth-stage larvae (L5) of A. cantonensis were investigated by next-generation sequencing (NGS). In the NGS database established from the larvae isolated from the brain of Sprague–Dawley rats, 31,487 unique genes with a mean length of 617 nucleotides were assembled. These genes were found to have a 46.08 % significant similarity to Caenorhabditis elegans by BLASTx. They were then compared with the expressed sequence tags of 18 other nematodes, and significant matches of 36.09–59.12 % were found. Among these genes, 3,338 were found to participate in 124 Kyoto Encyclopedia of Genes and Genomes pathways. These pathways included 1,514 metabolisms, 846 genetic information processing, 358 environmental information processing, 264 cellular processes, and 91 organismal systems. Analysis of 30,816 sequences with the gene ontology database indicated that their annotations included 5,656 biological processes (3,364 cellular processes, 3,061 developmental processes, and 3,191 multicellular organismal processes), 7,218 molecular functions (4,597 binding and 3,084 catalytic activities), and 4,719 cellular components (4,459 cell parts and 4,466 cells). Moreover, stress-related genes (112 heat stress and 33 oxidation stress) and genes for proteases (159) were not uncommon. This study is the first NGS-based study to set up a transcriptomic database of A. cantonensis L5. The results provide new insights into the survival, development, and host–parasite interactions of this blood-feeding nematode.Electronic supplementary materialThe online version of this article (doi:10.1007/s00436-013-3495-z) contains supplementary material, which is available to authorized users.

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Cathepsin B-like and hemoglobin-type cysteine proteases: Stage-specific gene expression in Angiostrongy cantonensis

Cited by 12 publications

References 33 publications

Immunolocalization and developmental expression patterns of two cathepsin B proteases (AC-cathB-1, -2) of Angiostrongylus cantonensis

Immunolocalization and developmental expression patterns of two cathepsin B proteases (AC-cathB-1, -2) of Angiostrongylus cantonensis

Screening and Functional Analysis of the Peroxiredoxin Specifically Expressed in Bursaphelenchus xylophilus—The Causative Agent of Pine Wilt Disease

Transcriptome profiling of the fifth-stage larvae of Angiostrongylus cantonensis by next-generation sequencing

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