Evidence map›Paper›PMID 27562899›Full record

ArticleParasitology research2016

Molecular and immunological characterization of cathepsin L-like cysteine protease of Paragonimus pseudoheterotremus.

Tippayarat Yoonuan, Supaporn Nuamtanong, Paron Dekumyoy, Orawan Phuphisut, Poom Adisakwattana

Abstract read
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Article in Parasitology research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.7field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Diagnosis of Human Trematode Infections.Advances in experimental medicine and biology · 2024
    Review
  4. Paragonimiasis.Advances in experimental medicine and biology · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
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  11. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Tippayarat YoonuanDepartment of Helminthology, Faculty of Tropical Medicine, Mahidol University, Ratchathewi, Bangkok, 10400, Thailand.
Supaporn NuamtanongDepartment of Helminthology, Faculty of Tropical Medicine, Mahidol University, Ratchathewi, Bangkok, 10400, Thailand.
Paron DekumyoyDepartment of Helminthology, Faculty of Tropical Medicine, Mahidol University, Ratchathewi, Bangkok, 10400, Thailand.
Orawan PhuphisutDepartment of Helminthology, Faculty of Tropical Medicine, Mahidol University, Ratchathewi, Bangkok, 10400, Thailand.
Poom AdisakwattanaDepartment of Helminthology, Faculty of Tropical Medicine, Mahidol University, Ratchathewi, Bangkok, 10400, Thailand. poom.adi@mahidol.ac.th.ORCID http://orcid.org/0000-0002-0313-9900
Mahidol University · TH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cathepsin L is a cysteine protease belonging to the papain family. In parasitic trematodes, cathepsin L plays essential roles in parasite survival and host-parasite interactions. In this study, cathepsin L of the lung fluke Paragonimus pseudoheterotremus (PpsCatL) was identified and its molecular biological and immunological features characterized. A sequence analysis of PpsCatL showed that the gene encodes a 325-amino-acid protein that is most similar to P. westermani cathepsin L. The in silico three-dimensional structure suggests that PpsCatL is a pro-enzyme that becomes active when the propeptide is cleaved. A recombinant pro-PpsCatL lacking the signal peptide (rPpsCatL), with a molecular weight of 35 kDa, was expressed in E. coli and reacted with P. pseudoheterotremus-infected rat sera. The native protein was detected in crude worm antigens and excretory-secretory products and was localized in the cecum and in the lamellae along the intestinal tract of the adult parasite. Enzymatic activity of rPpsCatL showed that the protein could cleave the fluorogenic substrate Z-Phe-Arg-AMC after autocatalysis but was inhibited with E64. The immunodiagnostic potential of the recombinant protein was evaluated with an enzyme-linked immunosorbent assay (ELISA) and suggested that rPpsCatL can detect paragonimiasis with high sensitivity and specificity (100 and 95.6 %, respectively). This supports the further development of an rPpsCatL-ELISA as an immunodiagnostic tool.

Indexed as

Amino Acid SequenceAnimalsAntigens, HelminthBase SequenceCathepsin LEnzyme-Linked Immunosorbent AssayEscherichia coliFemaleHelminth ProteinsHumansMiceModels, MolecularMolecular Sequence DataParagonimiasisParagonimusRatsAntigens, HelminthCathepsin LHelminth ProteinsCathepsin LCecumELISAEnzyme-linked immunosorbent assayParagonimus pseudoheterotremusRecombinant protein

Identifiers

PMID27562899
OpenAlexW2514040404

What OpenQuestion holds

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Registered trials

None linked

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.