Evidence map›Paper›PMID 22215189›Full record

ArticleParasitology research2012

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

Mei Cheng, Xiao Yang, Zhuoya Li, Hualiang He, Zhenyu Qu, Ai He, Zhongdao Wu, Ximei Zhan

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Article in Parasitology research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

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12citing papers in PubMed
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1 · What the graph read from it

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

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3 · Its place in the literature

Who cites it

12 citing papers in PubMed.

  1. Genome-Wide Analysis ofInternational journal of molecular sciences · 2023
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4 · The record

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5 · Who and what money

Authors and funding

8 authors.

Mei ChengDepartment of Parasitology, Zhongshan School of Medicine, Sun Yat-sen University, 74 2nd Zhongshan Road, Guangzhou, 510080, People's Republic of China.
Xiao Yang
Zhuoya Li
Hualiang He
Zhenyu Qu
Ai He
Zhongdao Wu
Ximei Zhan

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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.

Indexed as

Amino Acid SequenceAngiostrongylus cantonensisAnimalsCloning, MolecularCluster AnalysisCysteine ProteasesElectrophoresis, Polyacrylamide GelEnzyme StabilityFemaleGene Expression ProfilingGene LibraryHydrogen-Ion ConcentrationHydrolysisMaleMiceMice, Inbred BALB CCysteine ProteasesProteins

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.