Evidence map›Paper›PMID 30134158›Full record

ArticleCell reports2018

Site-Specific Glycosylation of Virion-Derived HIV-1 Env Is Mimicked by a Soluble Trimeric Immunogen.

Weston B Struwe, Elena Chertova, Joel D Allen, Gemma E Seabright, Yasunori Watanabe, David J Harvey, Max Medina-Ramirez, James D Roser, Rodman Smith, David Westcott and 6 more

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.

0numbers the graph read from it
0cells of the map it votes in
113citing papers in PubMed
11.5field-weighted citation impact, top 1% 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

113 citing papers in PubMed, 143 citations in OpenAlex.

  1. Article
  2. Article
  3. Canonical Antibodies Adopt Distinct Binding Modes to Recognize Viral Glycan Shields.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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  11. Review
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  15. Augmented humoral responses to HIV Env trimers delivered as transmembrane immunogens by self-replicating RNA.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
    Article
  16. Article
  17. Article
  18. Article
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  20. Article

53 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

16 authors at 6 institutions in 3 countries.

Weston B StruweOxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK; Chemistry Research Laboratory, Department of Chemistry, University of Oxford, 12 Mansfield Road, OX1 3TA, UK.
Elena ChertovaAIDS and Cancer Virus Program, Leidos Biomedical Research, Frederick National Laboratory for Cancer Research, Frederick, MD, USA.
Joel D AllenBiological Sciences and the Institute for Life Sciences, University of Southampton, Southampton SO17 1BJ, UK.
Gemma E SeabrightOxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK; Biological Sciences and the Institute for Life Sciences, University of Southampton, Southampton SO17 1BJ, UK.
Yasunori WatanabeOxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK; Biological Sciences and the Institute for Life Sciences, University of Southampton, Southampton SO17 1BJ, UK.
David J HarveyBiological Sciences and the Institute for Life Sciences, University of Southampton, Southampton SO17 1BJ, UK; Target Discovery Institute, Nuffield Department of Medicine, University of Oxford, Roosevelt Drive, Oxford OX3 7FZ, UK.
Max Medina-RamirezDepartment of Medical Microbiology, Academic Medical Center, University of Amsterdam, Amsterdam, the Netherlands.
James D RoserAIDS and Cancer Virus Program, Leidos Biomedical Research, Frederick National Laboratory for Cancer Research, Frederick, MD, USA.
Rodman SmithAIDS and Cancer Virus Program, Leidos Biomedical Research, Frederick National Laboratory for Cancer Research, Frederick, MD, USA.
David WestcottAIDS and Cancer Virus Program, Leidos Biomedical Research, Frederick National Laboratory for Cancer Research, Frederick, MD, USA.
Brandon F KeeleAIDS and Cancer Virus Program, Leidos Biomedical Research, Frederick National Laboratory for Cancer Research, Frederick, MD, USA.
Julian W BessAIDS and Cancer Virus Program, Leidos Biomedical Research, Frederick National Laboratory for Cancer Research, Frederick, MD, USA.
Rogier W SandersDepartment of Microbiology and Immunology, Weill Cornell Medical College, Cornell University, New York, NY, USA; Department of Medical Microbiology, Academic Medical Center, University of Amsterdam, Amsterdam, the Netherlands.
Jeffrey D LifsonAIDS and Cancer Virus Program, Leidos Biomedical Research, Frederick National Laboratory for Cancer Research, Frederick, MD, USA.
John P MooreDepartment of Microbiology and Immunology, Weill Cornell Medical College, Cornell University, New York, NY, USA. Electronic address: jpm2003@med.cornell.edu.
Max CrispinOxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, UK; Biological Sciences and the Institute for Life Sciences, University of Southampton, Southampton SO17 1BJ, UK. Electronic address: max.crispin@soton.ac.uk.
Leidos (United States) · USUniversity of Oxford · GBUniversity of Southampton · GBCornell University · USFrederick National Laboratory for Cancer Research · USAcademic Medical Center · NL

Funding

Support Component D/Vaccine Discovery, Concept to ClinicUM1AI100663 · NIAID · SCRIPPS RESEARCH INSTITUTE, THE · PI BAROUCH, DAN H. · 2012 to 2018
$131.5M
Structural studies of native-like SOSIP trimersP01AI110657 · NIAID · WEILL MEDICAL COLL OF CORNELL UNIV · PI MOORE, JOHN P · 2015 to 2024
$35.4M
CCR NIH HHS HHSN261200800001CNCI NIH HHS HHSN261200800001ENIAID NIH HHS P01 AI110657NIAID NIH HHS UM1 AI100663
6 · The paper itself

Abstract

Many broadly neutralizing antibodies (bnAbs) against HIV-1 recognize and/or penetrate the glycan shield on native, virion-associated envelope glycoprotein (Env) spikes. The same bnAbs also bind to recombinant, soluble trimeric immunogens based on the SOSIP design. While SOSIP trimers are close structural and antigenic mimics of virion Env, the extent to which their glycan structures resemble ones on infectious viruses is undefined. Here, we compare the overall glycosylation of gp120 and gp41 subunits from BG505 (clade A) virions produced in a lymphoid cell line with those from recombinant BG505 SOSIP trimers, including CHO-derived clinical grade material. We also performed detailed site-specific analyses of gp120. Glycans relevant to key bnAb epitopes are generally similar on the recombinant SOSIP and virion-derived Env proteins, although the latter do contain hotspots of elevated glycan processing. Knowledge of native versus recombinant Env glycosylation will guide vaccine design and manufacturing programs.

Indexed as

GlycosylationHIV-1HumansVirionenvelope glycoproteinglycosylationHIVmass spectrometry

Identifiers

PMID30134158
PMCPMC6113929
OpenAlexW2888011077

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.