Evidence map›Paper›PMID 25631795›Full record

ArticleJournal of clinical microbiology2015

Protein-peptide arrays for detection of specific anti-hepatitis D virus (HDV) genotype 1, 6, and 8 antibodies among HDV-infected patients by surface plasmon resonance imaging.

Marie-Bernadette Villiers, Jean-Claude Cortay, Sandra Cortès, Bénédicte Bloquel, Ségolène Brichler, Carine Brakha, Alan Kay, Nisrine Falah, Fabien Zoulim, Christophe Marquette and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of clinical microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.5field-weighted citation impact, top 17% 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

8 citing papers in PubMed, 11 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

12 authors at 6 institutions in 1 country.

Marie-Bernadette VilliersINSERM, U823, Grenoble, France Université Grenoble Alpes, Institut Albert Bonniot, Grenoble, France.
Jean-Claude CortayCentre National de Référence des Entérovirus, EA Site Laennec, Université Lyon 1, Lyon, France.
Sandra CortèsINSERM, U823, Grenoble, France Université Grenoble Alpes, Institut Albert Bonniot, Grenoble, France.
Bénédicte BloquelCentre National de Référence des Entérovirus, EA Site Laennec, Université Lyon 1, Lyon, France INSERM, U1052, UMR CNRS 5286, Centre de Recherche en Cancérologie de Lyon, Lyon, France.
Ségolène BrichlerService de Bactériologie, Virologie-Hygiène, Hôpital Avicenne, Groupe des Hôpitaux Universitaires Paris Seine Saint-Denis, Assistance Publique-Hôpitaux de Paris, Laboratoire Associé au Centre National de Référence des Hépatites B, C et delta, Bobigny, France Université Paris 13/Sorbonne Paris Cité, UFR Santé Médecine Biologie Humaine, Bobigny, France.
Carine BrakhaINSERM, U823, Grenoble, France Université Grenoble Alpes, Institut Albert Bonniot, Grenoble, France.
Alan KayINSERM, U1052, UMR CNRS 5286, Centre de Recherche en Cancérologie de Lyon, Lyon, France.
Nisrine FalahCentre National de Référence des Entérovirus, EA Site Laennec, Université Lyon 1, Lyon, France.
Fabien ZoulimINSERM, U1052, UMR CNRS 5286, Centre de Recherche en Cancérologie de Lyon, Lyon, France Hospices Civils Lyon, Lyon, France Université de Lyon 1, Lyon, France.
Christophe MarquetteUniversité de Lyon 1, Lyon, France Institut de Chimie et Biochimie Moléculaires et Supramoléculaires, Equipe Génie Enzymatique, Membranes Biomimétiques et Assemblages Supramoléculaires (GEMBAS), Université Lyon 1, CNRS 5246 ICBMS, Villeurbanne, Cedex, France.
Patrice N MarcheINSERM, U823, Grenoble, France Université Grenoble Alpes, Institut Albert Bonniot, Grenoble, France patrice.marche@inserm.fr paul.deny@inserm.fr.
Paul DényINSERM, U1052, UMR CNRS 5286, Centre de Recherche en Cancérologie de Lyon, Lyon, France Service de Bactériologie, Virologie-Hygiène, Hôpital Avicenne, Groupe des Hôpitaux Universitaires Paris Seine Saint-Denis, Assistance Publique-Hôpitaux de Paris, Laboratoire Associé au Centre National de Référence des Hépatites B, C et delta, Bobigny, France Université Paris 13/Sorbonne Paris Cité, UFR Santé Médecine Biologie Humaine, Bobigny, France patrice.marche@inserm.fr paul.deny@inserm.fr.
Inserm · FRUniversité Claude Bernard Lyon 1 · FRInstitut pour l'avancée des biosciences · FRSorbonne Paris Cité · FRUniversité Grenoble Alpes · FRUniversité Paris Cité · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Liver diseases linked to hepatitis B-hepatitis D virus co- or superinfections are more severe than those during hepatitis B virus (HBV) monoinfection. The diagnosis of hepatitis D virus (HDV) infection therefore remains crucial in monitoring patients but is often overlooked. To integrate HDV markers into high-throughput viral hepatitis diagnostics, we studied the binding of anti-HDV antibodies (Abs) using surface plasmon resonance imaging (SPRi). We focused on the ubiquitous HDV genotype 1 (HDV1) and the more uncommon African-HDV6 and HDV8 genotypes to define an array with recombinant proteins or peptides. Full-length and truncated small hepatitis D antigen (S-HDAg) recombinant proteins of HDV genotype 1 (HDV1) and 11 HDV peptides of HDV1, 6, and 8, representing various portions of the delta antigen were grafted onto biochips, allowing SPRi measurements to be made. Sixteen to 17 serum samples from patients infected with different HDV genotypes were injected onto protein and peptide chips. In all, Abs against HDV proteins and/or peptides were detected in 16 out of 17 infected patients (94.12%), although the amplitude of the SPR signal varied. The amino-terminal part of the protein was poorly immunogenic, while epitope 65-80, exposed on the viral ribonucleoprotein, may be immunodominant, as 9 patient samples led to a specific SPR signal on peptide 65 type 1 (65#1), independently of the infecting genotype. In this pilot study, we confirmed that HDV infection screening based on the reactivity of patient Abs against carefully chosen HDV peptides and/or proteins can be included in a syndrome-based viral hepatitis diagnostic assay. The preliminary results indicated that SPRi studying direct physical HDAg-anti-HDV Ab interactions was more convenient using linear peptide epitopes than full-length S-HDAg proteins, due to the regeneration process, and may represent an innovative approach for a hepatitis syndrome-viral etiology-exploring array.

Indexed as

AdolescentAdultAmino Acid SequenceHepatitis AntibodiesHepatitis DHepatitis delta AntigensHepatitis Delta VirusHumansMiddle AgedMolecular Sequence DataPilot ProjectsProtein Array AnalysisSequence AlignmentSurface Plasmon ResonanceYoung AdultHepatitis AntibodiesHepatitis delta Antigens

Identifiers

PMID25631795
PMCPMC4365268
OpenAlexW2115295376

What OpenQuestion holds

Textmetadata
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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.