Evidence map›Paper›PMID 25885535›Full record

ArticleJournal of translational medicine2015

A chimeric EBV gp350/220-based VLP replicates the virion B-cell attachment mechanism and elicits long-lasting neutralizing antibodies in mice.

Javier Gordon Ogembo, Matthew R Muraswki, Lori W McGinnes, Agapi Parcharidou, Rujapak Sutiwisesak, Timelia Tison, Juan Avendano, Deep Agnani, Robert W Finberg, Trudy G Morrison and 1 more

Open access · goldAbstract read
In one paragraph

Article in Journal of translational medicine, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed, 1 pooled it
2.7field-weighted citation impact, top 8% 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

39 citing papers in PubMed, 1 synthesis or guideline pooled it, 77 citations in OpenAlex.

  1. Pooled it
  2. Chemical reviews · 2026
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  20. Overview of virus and cancer relationships. Position paper.Revista espanola de quimioterapia : publicacion oficial de la Sociedad Espanola de Quimioterapia · 2021
    Article
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

11 authors at 3 institutions in 1 country.

Javier Gordon OgemboDepartment of Medicine, University of Massachusetts Medical School, 364 Plantation Street, LRB Room 323, Worcester, MA, 01605, USA. javier.ogembo@umassmed.edu.
Matthew R MuraswkiDepartment of Medicine, Beth Israel Deaconess Medical Center/Harvard Medical School, Boston, MA, UK. mrmurawsk@gmail.com.
Lori W McGinnesDepartment of Microbiology and Physiological Systems, University of Massachusetts Medical School, Worcester, MA, USA. lori.mcginnes@umassmed.edu.
Agapi ParcharidouDepartment of Medicine, Beth Israel Deaconess Medical Center/Harvard Medical School, Boston, MA, UK. agapi.parcharidou@bedfordhospital.nhs.uk.
Rujapak SutiwisesakDepartment of Medicine, University of Massachusetts Medical School, 364 Plantation Street, LRB Room 323, Worcester, MA, 01605, USA. rujapak.sutiwisesak@umassmed.edu.
Timelia TisonDepartment of Medicine, University of Massachusetts Medical School, 364 Plantation Street, LRB Room 323, Worcester, MA, 01605, USA. timelia.tison@umassmed.edu.
Juan AvendanoDepartment of Medicine, Beth Israel Deaconess Medical Center/Harvard Medical School, Boston, MA, UK. juanmanuelavendano@icloud.com.
Deep AgnaniDepartment of Medicine, Beth Israel Deaconess Medical Center/Harvard Medical School, Boston, MA, UK. dagnani@gmail.com.
Robert W FinbergDepartment of Medicine, University of Massachusetts Medical School, 364 Plantation Street, LRB Room 323, Worcester, MA, 01605, USA. robert.finberg@umassmed.edu.
Trudy G MorrisonDepartment of Microbiology and Physiological Systems, University of Massachusetts Medical School, Worcester, MA, USA. trudy.morrison@umassmed.edu.
Joyce D FingerothDepartment of Medicine, University of Massachusetts Medical School, 364 Plantation Street, LRB Room 323, Worcester, MA, 01605, USA. joyce.fingeroth@umassmed.edu.
University of Massachusetts Chan Medical School · USHarvard University · USBeth Israel Deaconess Medical Center · US

Funding

Formins (FHOS) in CD21-mediated signaling &virus entryR01AI063571 · NIAID · BETH ISRAEL DEACONESS MEDICAL CENTER · PI FINGEROTH, JOYCE DIANE · 2005 to 2009
$1.9M
Unmasking the roles of KSHV glycoproteins in virus entry and vaccine developmentK01CA184388 · NCI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI OGEMBO, JAVIER GORDON · 2014 to 2018
$536k
Humoral Immune Responses to Virus-like Particle Vaccine Candidates for RSVR56AI093791 · NIAID · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI MORRISON, TRUDY G. · 2011 to 2011
$411k
NCI NIH HHS CA184388-01NCI NIH HHS K01 CA184388NIAID NIH HHS R01 AI063571NIAID NIH HHS R01AI063571NIAID NIH HHS R56 AI093791
6 · The paper itself

Abstract

Epstein-Barr virus (EBV), an oncogenic gammaherpesvirus, causes acute infectious mononucleosis (AIM) and is linked to the development of several human malignancies. There is an urgent need for a vaccine that is safe, prevents infection and/or limits disease. Unique among human herpesviruses, glycoprotein (gp)350/220, which initiates EBV attachment to susceptible host cells, is the major ligand on the EBV envelope and is highly conserved. Interaction between gp350/220 and complement receptor type 2 (CR2)/CD21 and/or (CR1)/CD35 on B-cells is required for infection. Potent antibody responses to gp350/220 occur in animal models and humans. Thus, gp350/220 provides an attractive candidate for prophylactic subunit vaccine development. However, in a recent Phase II clinical trial immunization with soluble recombinant gp350 reduced the incidence of AIM, but did not prevent infection. Despite various attempts to produce an EBV vaccine, no vaccine is licensed. Herein we describe a sub-unit vaccine against EBV based on a novel Newcastle disease virus (NDV)-virus-like particle (VLP) platform consisting of EBVgp350/220 ectodomain fused to NDV-fusion (F) protein. The chimeric protein EBVgp350/220-F is incorporated into the membrane of a VLP composed of the NDV matrix and nucleoprotein. The particles resemble native EBV in diameter and shape and bind CD21 and CD35. Immunization of BALB/c mice with EBVgp350/220-F VLPs elicited strong, long-lasting neutralizing antibody responses when assessed in vitro. This chimeric VLP is predicted to provide a superior safety profile as it is efficiently produced in Chinese hamster ovary (CHO) cells using a platform devoid of human nucleic acid and EBV-transforming genes.

Indexed as

AnimalsAntibodies, NeutralizingAntigens, CDB-LymphocytesCell AdhesionCell LineHumansImmunizationImmunoglobulin GMice, Inbred BALB CNeutralization TestsProtein BindingRecombinant ProteinsViral Matrix ProteinsVirionAntibodies, NeutralizingAntigens, CDEBV-associated membrane antigen, Epstein-Barr virusImmunoglobulin GRecombinant ProteinsViral Matrix Proteins

Identifiers

PMID25885535
PMCPMC4328182
OpenAlexW2097420026

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.