Evidence map›Paper›PMID 30878092›Full record

ArticleVeterinary parasitology2019

Characterization of a novel cathepsin L-like protease from Taenia solium metacestodes for the immunodiagnosis of porcine cysticercosis.

Nancy León-Janampa, Ruddy Liendo, Robert H Gilman, Carlos Padilla, Hector H García, Armando Gonzales, Patricia Sheen, Mónica J Pajuelo, Mirko Zimic, Cysticercosis Working Group in Perú

Abstract read
In one paragraph

Article in Veterinary parasitology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

6 citing papers in PubMed, 9 citations in OpenAlex.

  1. Systematic Evaluation of Four Cysteine Proteases (Tropical medicine and infectious disease · 2026
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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

10 authors at 5 institutions in 2 countries.

Nancy León-JanampaLaboratorio de Bioinformática y Biología Molecular, Facultad de Ciencias y Filosofía, Universidad Peruana Cayetano Heredia, Lima, Peru. Electronic address: nancy.leon.j@upch.pe.
Ruddy LiendoLaboratorio de Bioinformática y Biología Molecular, Facultad de Ciencias y Filosofía, Universidad Peruana Cayetano Heredia, Lima, Peru. Electronic address: ruddy.liendo.p@upch.pe.
Robert H GilmanDepartment of International Health, Johns Hopkins Bloomberg School of Public Health, Baltimore, Maryland, USA. Electronic address: gilmanbob@gmail.com.
Carlos PadillaInstituto Nacional de Salud, Lima, Peru. Electronic address: cpadillar@hotmail.com.
Hector H GarcíaCysticercosis Unit, Instituto de Ciencias Neurológicas, Lima, Peru. Electronic address: hgarcia1@jhu.edu.
Armando GonzalesSchool of Veterinary Medicine, Universidad Nacional Mayor de San Marcos, Lima, Peru. Electronic address: agonza41@jhu.edu.
Patricia SheenLaboratorio de Bioinformática y Biología Molecular, Facultad de Ciencias y Filosofía, Universidad Peruana Cayetano Heredia, Lima, Peru. Electronic address: patricia.sheen@upch.pe.
Mónica J PajueloLaboratorio de Bioinformática y Biología Molecular, Facultad de Ciencias y Filosofía, Universidad Peruana Cayetano Heredia, Lima, Peru; Department of International Health, Johns Hopkins Bloomberg School of Public Health, Baltimore, Maryland, USA. Electronic address: monica.pajuelo.t@upch.pe.
Mirko ZimicLaboratorio de Bioinformática y Biología Molecular, Facultad de Ciencias y Filosofía, Universidad Peruana Cayetano Heredia, Lima, Peru. Electronic address: mirko.zimic@upch.pe.
Cysticercosis Working Group in Perú
Universidad Peruana Cayetano Heredia · PEJohns Hopkins University · USInstituto Nacional de Enfermedades Neoplásicas · PEInstituto Nacional de Salud · PENational University of San Marcos · PE

Funding

Training in Parasitic Diseases and Central Nervous System Infections in Peru.D43TW001140 · FIC · UNIVERSIDAD PERUANA CAYETANO HEREDIA · PI GARCIA, HECTOR HUGO, GILMAN, ROBERT H · 1999 to 2025
$5.7M
Infectious Diseases Training program in Bolivia: South-South Training with PeruD43TW010074 · FIC · JOHNS HOPKINS UNIVERSITY · PI ROBERT H GILMAN, Jeffrey Tornheim · 2015 to 2026
$3.5M
Scientific CoreU19AI129909 · NIAID · UNIVERSIDAD PERUANA CAYETANO HEREDIA · PI GONZALEZ, ARMANDO EMILIANO · 2017 to 2021
$2.8M
FIC NIH HHS D43 TW001140FIC NIH HHS D43 TW010074NIAID NIH HHS U19 AI129909
6 · The paper itself

Abstract

Porcine cysticercosis is an endemic parasitic disease caused by infection with Taenia solium that is found predominantly in developing countries. In order to aid in the development of simple diagnostic approaches, identification and characterization of potential new antigens for immunodiagnostic purposes is desired. The cysteine protease family has previously been found to have important immunodiagnostic properties. These proteases are expressed as zymogens which contain a signal peptide, pro-peptide, and an active domain. Subsequent catalytic cleavage of the pro-peptide converts these zymogens into enzymes. With the use of bioinformatic tools we identified an active domain of a novel cathepsin L-like cysteine protease (TsolCL) in the T. solium genome. The TsolCL gene includes 705 nucleotides (nt) within a single intron and a 633 nt exonic sequence encoding an active protein of 211 amino acids. Sequence alignment and phylogenetic analysis suggest that the TsolCL gene is closely related to genes found in Echinoccocus granulosus and E. multiloculars. In addition, TsolCL was found to have a 61.9%-99.0% similarity to other cathepsin L proteins found in other helminths and mammals. We cloned, expressed, purified, and characterized the recombinant active TsolCL (27 kDa) using the baculovirus-insect cell expression system. TsolCL showed cysteine protease enzymatic activity with the capacity to hydrolyze the Z-Phe-Arg-AMC substrate as well as bovine serum albumin. However, TsolCL was not able to hydrolyze human immunoglobulin. In addition, TsolCL has cathepsin L conserved amino acid residues in the catalytic site (Gln8, Cys14, His159, Asn179 and Trp181) and the motif GCNGG. Using ELISA, TsolCL was able to distinguish circulating IgG antibodies between healthy animals and naturally infected pigs with cysticercosis, showing a moderate sensitivity of 83.33% (40/48; 95% CI: [69.8%-92.5 %]), and a specificity of 83.78% (31/37; 95% CI: [67.9%-93.8%]). In conclusion, a novel cathepsin L-like cysteine protease from a T. solium metacestode was expressed successfully in Baculovirus system and was evaluated as a candidate antigen to diagnose porcine cysticercosis using the ELISA immunoassay.

Indexed as

AnimalsAntibodies, HelminthAntigens, HelminthBaculoviridaeCathepsin LCysticercosisEnzyme-Linked Immunosorbent AssayImmunoglobulin GImmunologic TestsPhylogenyRecombinant ProteinsSf9 CellsSwineSwine DiseasesTaenia soliumAntibodies, HelminthAntigens, HelminthCathepsin LImmunoglobulin GRecombinant ProteinsBaculovirus expression vector systemCathepsin LCysticercosisImmunodiagnosisTaenia solium

Identifiers

PMID30878092
PMCPMC7010362
OpenAlexW2912596584

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Registered trials

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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.