Evidence map›Paper›PMID 26942007›Full record

ArticleHepatitis research and treatment2016

A Novel Structurally Stable Multiepitope Protein for Detection of HCV.

Alexsandro S Galdino, José C Santos, Marilen Q Souza, Yanna K M Nóbrega, Mary-Ann E Xavier, Maria S S Felipe, Sonia M Freitas, Fernando A G Torres

Open access · hybridAbstract read
In one paragraph

Article in Hepatitis research and treatment, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

7 citing papers in PubMed, 18 citations in OpenAlex.

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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

8 authors at 2 institutions in 1 country.

Alexsandro S GaldinoLaboratório de Biotecnologia de Microrganismos, Universidade Federal de São João Del-Rei, 35501-296 Divinópolis, MG, Brazil.
José C SantosDepartamento de Biologia Celular, Universidade de Brasília, 70910-900 Brasília, DF, Brazil.
Marilen Q SouzaDepartamento de Biologia Celular, Universidade de Brasília, 70910-900 Brasília, DF, Brazil.
Yanna K M NóbregaLaboratório de Doenças Imunogenéticas e Crônico-degenerativas, Universidade de Brasília, 70910-900 Brasília, DF, Brazil.
Mary-Ann E XavierLaboratório de Biofísica, Universidade de Brasília, 70910-900 Brasília, DF, Brazil.
Maria S S FelipeDepartamento de Biologia Celular, Universidade de Brasília, 70910-900 Brasília, DF, Brazil.
Sonia M FreitasLaboratório de Biofísica, Universidade de Brasília, 70910-900 Brasília, DF, Brazil.
Fernando A G TorresDepartamento de Biologia Celular, Universidade de Brasília, 70910-900 Brasília, DF, Brazil.
Universidade de Brasília · BRFederal University of São João del-Rei · BR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hepatitis C virus (HCV) has emerged as the major pathogen of liver diseases in recent years leading to worldwide blood-transmitted chronic hepatitis, liver cirrhosis, and hepatocellular carcinoma. Accurate diagnosis for differentiation of hepatitis C from other viruses is thus of pivotal importance for proper treatment. In this work we developed a recombinant multiepitope protein (rMEHCV) for hepatitis C diagnostic purposes based on conserved and immunodominant epitopes from core, NS3, NS4A, NS4B, and NS5 regions of the virus polyprotein of genotypes 1a, 1b, and 3a, the most prevalent genotypes in South America (especially in Brazil). A synthetic gene was designed to encode eight epitopes in tandem separated by a flexible linker and bearing a his-tag at the C-terminal end. The recombinant protein was produced in Escherichia coli and purified in a single affinity chromatographic step with >95% purity. Purified rMEHCV was used to perform an ELISA which showed that the recombinant protein was recognized by IgG and IgM from human serum samples. The structural data obtained by circular dichroism (CD) spectroscopy showed that rMEHCV is a highly thermal stable protein at neutral and alkaline conditions. Together, these results show that rMEHCV should be considered an alternative antigen for hepatitis C diagnosis.

Identifiers

PMID26942007
PMCPMC4749800
OpenAlexW2290571398

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.