Evidence map›Paper›PMID 26365435›Full record

ArticleNature communications2015

Structure of HCMV glycoprotein B in the postfusion conformation bound to a neutralizing human antibody.

Sumana Chandramouli, Claudio Ciferri, Pavel A Nikitin, Stefano Caló, Rachel Gerrein, Kara Balabanis, James Monroe, Christy Hebner, Anders E Lilja, Ethan C Settembre and 1 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.

0numbers the graph read from it
0cells of the map it votes in
90citing papers in PubMed
8.9field-weighted citation impact, top 2% 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

90 citing papers in PubMed, 134 citations in OpenAlex.

  1. Trial
  2. Trial
  3. HCMV glycoprotein B subunit vaccine efficacy mediated by nonneutralizing antibody effector functions.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Trial
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Structure and Antigenicity of Kaposi's Sarcoma-Associated Herpesvirus Glycoprotein B.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Computational design of prefusion-stabilized Herpesvirus gB trimers.bioRxiv : the preprint server for biology · 2024
    Article
  20. Article

30 more citing papers are in PubMed but not listed here.

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 2 institutions in 2 countries.

Sumana ChandramouliGSK Vaccines, 45 Sidney Street, Cambridge, Massachusetts 02139, USA.
Claudio CiferriGSK Vaccines, 45 Sidney Street, Cambridge, Massachusetts 02139, USA.
Pavel A NikitinNovartis Institutes for Biomedical Research, Emeryville, California 94608, USA.
Stefano CalóGSK Vaccines, Via Fiorentina 1, Siena 53100, Italy.
Rachel GerreinGSK Vaccines, 45 Sidney Street, Cambridge, Massachusetts 02139, USA.
Kara BalabanisGSK Vaccines, 45 Sidney Street, Cambridge, Massachusetts 02139, USA.
James MonroeGSK Vaccines, 45 Sidney Street, Cambridge, Massachusetts 02139, USA.
Christy HebnerNovartis Institutes for Biomedical Research, Emeryville, California 94608, USA.
Anders E LiljaGSK Vaccines, 45 Sidney Street, Cambridge, Massachusetts 02139, USA.
Ethan C SettembreNovartis Influenza Vaccines, 45 Sidney Street, Cambridge, Massachusetts 02139, USA.
Andrea CarfiGSK Vaccines, 45 Sidney Street, Cambridge, Massachusetts 02139, USA.
Novartis (United States) · USToscana Life Sciences · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human cytomegalovirus (HCMV) poses a significant threat to immunocompromised individuals and neonates infected in utero. Glycoprotein B (gB), the herpesvirus fusion protein, is a target for neutralizing antibodies and a vaccine candidate due to its indispensable role in infection. Here we show the crystal structure of the HCMV gB ectodomain bound to the Fab fragment of 1G2, a neutralizing human monoclonal antibody isolated from a seropositive subject. The gB/1G2 interaction is dominated by aromatic residues in the 1G2 heavy chain CDR3 protruding into a hydrophobic cleft in the gB antigenic domain 5 (AD-5). Structural analysis and comparison with HSV gB suggest the location of additional neutralizing antibody binding sites on HCMV gB. Finally, immunoprecipitation experiments reveal that 1G2 can bind to HCMV virion gB suggesting that its epitope is exposed and accessible on the virus surface. Our data will support the development of vaccines and therapeutic antibodies against HCMV infection.

Indexed as

Antibodies, NeutralizingAntibodies, ViralAntigens, ViralCrystallizationCrystallography, X-RayCytomegalovirusHumansImmunoglobulin Fab FragmentsImmunoprecipitationMicroscopy, ElectronMutagenesis, Site-DirectedProtein ConformationViral Envelope ProteinsViral Fusion ProteinsAntibodies, NeutralizingAntibodies, ViralAntigens, Viralglycoprotein B, SimplexvirusImmunoglobulin Fab FragmentsViral Envelope ProteinsViral Fusion Proteins

Identifiers

PMID26365435
PMCPMC4579600
OpenAlexW2262975933

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.