Preliminary molecular characterization of the human pathogen Angiostrongylus cantonensis

He, Hualiang; Cheng, Minquan; Xiao, Yang; Meng, Jinxiu; He, Anbang; Zheng, Xiaoying; Li, Zhuoya; Guo, Pengjuan; ZhiHua, Pan; Zhan, Xi

doi:10.1186/1471-2199-10-97

Cited by 21 publications

(17 citation statements)

References 56 publications

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“…Characterization of the functions of these encoded proteins by Gene Ontology analysis showed enrichment in proteins with binding and catalytic activity. The observed pattern of enzymes involved in protein metabolism, lipid metabolism, and glycolysis may reflect the central nervous system habitat of this pathogen (He et al 2009). There are many genes of A. cantonensis having been cloned and analyzed.…”

Section: Molecular Biology Of a Cantonensismentioning

confidence: 98%

Angiostrongylus cantonensis in China

Wei

2013

Treatment of Human Parasitosis in Traditional Chinese Medicine

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Section: Molecular Biology Of a Cantonensismentioning

confidence: 98%

Angiostrongylus cantonensis in China

Wei

2013

Treatment of Human Parasitosis in Traditional Chinese Medicine

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“…Recently, with the analysis the sequences of ∼1,200 clones of A. cantonensis fourth-stage larvae cDNA library (He et al 2009), we have identified a novel cystatin homologue, named AcCystatin. The 369-bp ORF encoded for 120 amino acid residues with a predicted molecular mass of 13,580.34 Da and an isoelecric point (pI) value of 5.85.…”

Section: Cloning and Sequence Analysismentioning

confidence: 98%

“…Cystatins of parasitic nematodes are well-described pathogenicity factors contributing to downregulation of T-cell proliferation of their hosts and induce anti-inflammatory cytokine responses (Zavasnik-Bergant 2008). Cystatin has also been identified in the nematode A. cantonensis in our previous study (He et al 2009), but the biological functions remain unknown.…”

Section: Introductionmentioning

confidence: 94%

Molecular cloning and characterization of cystatin, a cysteine protease inhibitor, from Angiostrongylus cantonensis

Liu

Han

et al. 2010

Parasitol Res

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Cystatins are thiol proteinase inhibitors ubiquitously present in mammalian body and serve various important physiological functions. In the present study, a novel cystatin molecule (AcCystatin) was cloned from a cDNA library of Angiostrongylus cantonensis fourth-stage larvae. The putative 14-kDa protein contained 120 residues with cystatin-conserved motifs known to interact with the active site of cysteine peptidases and showed high identities with cystatins from other nematodes. RT-PCR analysis revealed that the expression pattern of AcCystatin was equal at the time points of third-stage larvae, fourth-stage larvae, and adults of the parasite life cycle. The recombinant AcCystatin (rAcCystatin) expressed and purified from Escherichia coli has been demonstrated to possess an obvious inhibitory activity against cathepsin B and could significantly upregulate nitric oxide production from IFN-gamma activated RAW 264.7 macrophages. Sera from mice (non-permissive host) infected with A. cantonensis detected rAcCystatin by Western blot, while the sera from infected rats (permissive host) could not. The results implied that AcCystatin might be an immunoregulator in A. cantonensis infection.

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“…Identification of AcCBL1 from A. cantonensis fourth-stage larvae cDNA library and sequence analysis A cDNA library of A. cantonensis fourth-stage larvae was constructed and sequenced by expressed sequence tag method (He et al 2009). About 1,200 clones were sequenced, and bioinformatics analysis revealed 378 cDNA clusters, and 168 cDNAs contained open reading frame.…”

Section: Parasitesmentioning

confidence: 99%

Cloning and characterization of a novel cathepsin B-like cysteine proteinase from Angiostrongylus cantonensis

Cheng

Xiao²,

Li³

et al. 2012

Parasitol Res

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Cysteine protease plays a key role in host-parasite interactions. In this study, we identified a novel gene encoding a cathepsin B-like cysteine protease (AcCBL1) from the cDNA library of Angiostrongysus cantonensis fourth-stage larvae (L4) and characterized its biological role in the parasite. Sequence and phylogeny analysis showed that AcCBL1 is related to other cathepsin B family members with the conserved catalytic triad (Cys, His, Asn) and diagnostic occluding loop. In addition, the sequence contains a specific "hemoglobinase motif" and might have a hemoglobinase (Hb)-degrading function. The recombinant AcCBL1 (rAcCBL1) exhibited the protease activity by gelation SDS/PAGE assay; rAcCBL1 can cleave the fluorogenic substrate Z-Arg-Arg-AMC, and the optimum pH was 5.5. The enzyme can hydrolyse several host proteins including Hb and human IgG in acidic pH, but low levels of hydrolysis were observed in neutral pH. Reverse transcription polymerase chain reaction revealed that AcCBL1 expression was detected throughout various developmental stages, L3, L4, adult male and female worms. Western blotting analysis indicated that AcCBL1 was an excretory/secretory product of L4 in mature form of protease. Immunolocalization demonstrated that AcCBL1 was mainly localized in the intestine of L4. These results suggest that rAcCBL1 may play an important role in the parasite nutrition uptake.

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Preliminary molecular characterization of the human pathogen Angiostrongylus cantonensis

Cited by 21 publications

References 56 publications

Angiostrongylus cantonensis in China

Angiostrongylus cantonensis in China

Molecular cloning and characterization of cystatin, a cysteine protease inhibitor, from Angiostrongylus cantonensis

Cloning and characterization of a novel cathepsin B-like cysteine proteinase from Angiostrongylus cantonensis

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