Evidence map›Paper›PMID 30587198›Full record

ArticleVirology journal2018

Optimization of Zika virus envelope protein production for ELISA and correlation of antibody titers with virus neutralization in Mexican patients from an arbovirus endemic region.

Young Chan Kim, Cesar Lopez-Camacho, Joanne E Nettleship, Nahid Rahman, Michelle L Hill, Laura Silva-Reyes, Georgina Ortiz-Martinez, Gloria Figueroa-Aguilar, María Antonieta Mar, Héctor Vivanco-Cid and 5 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Virology journal, 2018. 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
2.3field-weighted citation impact, top 11% 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, 14 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

15 authors at 7 institutions in 2 countries.

Young Chan KimThe Jenner Institute, Nuffield Department of Medicine, The Henry Wellcome Building for Molecular Physiology, University of Oxford, Old Road Campus Research Building. Roosevelt Drive, Oxford, OX3 7DQ, UK.
Cesar Lopez-CamachoThe Jenner Institute, Nuffield Department of Medicine, The Henry Wellcome Building for Molecular Physiology, University of Oxford, Old Road Campus Research Building. Roosevelt Drive, Oxford, OX3 7DQ, UK.
Joanne E NettleshipDivision of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, UK.
Nahid RahmanDivision of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, UK.
Michelle L HillOxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Laura Silva-ReyesOxford Vaccine Group, Department of Paediatrics, University of Oxford and the NIHR Oxford Biomedical Research Centre, Centre for Clinical Vaccinology and Tropical Medicine, Churchill Hospital, Oxford, UK.
Georgina Ortiz-MartinezLaboratorio de Hemostasia y Biología Vascular. División de Estudios de Posgrado. Facultad de Ciencias Médicas y Biológicas "Dr. Ignacio Chávez", Universidad Michoacana de San Nicolás de Hidalgo, UMSNH, Morelia, Mexico.
Gloria Figueroa-AguilarLaboratorio Estatal de Salud Pública, Secretaría de Salud de Michoacán, Morelia, Michoacán, Mexico.
María Antonieta MarHGZMF No. 12 Lázaro Cárdenas Michoacán dirección av. Lázaro Cárdenas No. 154 Col. Centro Lázaro Cárdenas Michoacán, Veracruz, Mexico.
Héctor Vivanco-CidInstituto de Investigaciones Médico-Biológicas, Universidad Veracruzana, Veracruz, Mexico.
Christine S RollierOxford Vaccine Group, Department of Paediatrics, University of Oxford and the NIHR Oxford Biomedical Research Centre, Centre for Clinical Vaccinology and Tropical Medicine, Churchill Hospital, Oxford, UK.
Nicole ZitzmannOxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Martha Eva Viveros-SandovalLaboratorio de Hemostasia y Biología Vascular. División de Estudios de Posgrado. Facultad de Ciencias Médicas y Biológicas "Dr. Ignacio Chávez", Universidad Michoacana de San Nicolás de Hidalgo, UMSNH, Morelia, Mexico.
Raymond J OwensDivision of Structural Biology, Wellcome Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford, UK.
Arturo Reyes-SandovalThe Jenner Institute, Nuffield Department of Medicine, The Henry Wellcome Building for Molecular Physiology, University of Oxford, Old Road Campus Research Building. Roosevelt Drive, Oxford, OX3 7DQ, UK. arturo.reyes@ndm.ox.ac.uk.ORCID 0000-0002-2648-1696
University of Oxford · GBRutherford Appleton Laboratory · GBChurchill Hospital · GBUniversidad Michoacana de San Nicolás de Hidalgo · MXCentre for Human Genetics · GBSecretaria de Salud · MXUniversidad Veracruzana · MX

Funding

Department of HealthMedical Research Council MR/K018779/1
6 · The paper itself

Abstract

backgroundZika virus (ZIKV) has become a global threat with immediate need for accurate diagnostics, efficacious vaccines and therapeutics. Several ZIKV envelope (Env)-based vaccines have been developed recently. However, many commercially available ZIKV Env are based on the African lineage and produced in insect cells. Here, we sought to produce Asian-lineage ZIKV Env in mammalian cells for research and clinical applications.

methodsWe designed various gene expression constructs to optimize the production of ZIKV using prM-Env and full or C-terminal truncations of Env; with or without a rat CD4 fusion partner to allow large-scale production of soluble protein in mammalian HEK293 cells. Protein expression was verified by mass spectrometry and western-blot with a pan-flavivirus antibody, a ZIKV Env monoclonal antibody and with immune sera from adenoviral (ChAdOx1) ZIKV Env-vaccinated mice. The resulting Env-CD4 was used as a coating reagent for immunoassay (ELISA) using both mouse and human seropositive sera.

resultsReplacement of the C-terminus transmembrane Env domain by a rat CD4 and addition of prM supported optimal expression and secretion of Env. Binding between the antigens and the antibodies was similar to binding when using commercially available ZIKV Env reagents. Furthermore, antibodies from ZIKV patients bound ZIKV Env-CD4 in ELISA assays, whereas sera from healthy blood donors yielded minimal OD background. The serological outcomes of this assay correlated also with ZIKV neutralisation capacity in vitro.

conclusionsResults obtained from this study indicate the potential of the Asian-lineage Zika Env-CD4 and Env proteins in ELISA assays to monitor humoral immune responses in upcoming clinical trials as well as a sero-diagnostic tool in ZIKV infection.

Indexed as

AnimalsAntibodies, NeutralizingAntibodies, ViralCD4 AntigensEnzyme-Linked Immunosorbent AssayHEK293 CellsHumansMexicoMiceNeutralization TestsRatsRecombinant Fusion ProteinsViral Envelope ProteinsZika VirusAntibodies, NeutralizingAntibodies, ViralCD4 AntigensRecombinant Fusion ProteinsViral Envelope ProteinsCD4 fusion tagELISAEnvelope proteinMexican patientsNeutralizing antibodiesProtein productionZika virus

Identifiers

PMID30587198
PMCPMC6307127
OpenAlexW2908477962

What OpenQuestion holds

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LicenceCC BY
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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.