Evidence map›Paper›PMID 27807235›Full record

ArticleJournal of virology2017

Molecular Architecture of the Cleavage-Dependent Mannose Patch on a Soluble HIV-1 Envelope Glycoprotein Trimer.

Anna-Janina Behrens, David J Harvey, Emilia Milne, Albert Cupo, Abhinav Kumar, Nicole Zitzmann, Weston B Struwe, John P Moore, Max Crispin

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
5.8field-weighted citation impact, top 4% 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

68 citing papers in PubMed, 91 citations in OpenAlex.

  1. Article
  2. Review
  3. From sequence to scaffold: Computational design of protein nanoparticle vaccines from AlphaFold2-predicted building blocks.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  4. Review
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  6. 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
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Variations inBiomolecules · 2023
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review

8 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

9 authors at 3 institutions in 2 countries.

Anna-Janina BehrensOxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford, United Kingdom.
David J HarveyOxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford, United Kingdom.
Emilia MilneOxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford, United Kingdom.
Albert CupoDepartment of Microbiology and Immunology, Weill Cornell Medical College, New York, New York, USA.
Abhinav KumarOxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford, United Kingdom.
Nicole ZitzmannOxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford, United Kingdom.
Weston B StruweOxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford, United Kingdom.
John P MooreDepartment of Microbiology and Immunology, Weill Cornell Medical College, New York, New York, USA.
Max CrispinOxford Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford, United Kingdom max.crispin@bioch.ox.ac.uk.
University of Oxford · GBCornell University · USScripps Research Institute · US

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
NIAID NIH HHS P01 AI110657NIAID NIH HHS UM1 AI100663
6 · The paper itself

Abstract

The formation of a correctly folded and natively glycosylated HIV-1 viral spike is dependent on protease cleavage of the gp160 precursor protein in the Golgi apparatus. Cleavage induces a compact structure which not only renders the spike capable of fusion but also limits further maturation of its extensive glycosylation. The redirection of the glycosylation pathway to preserve underprocessed oligomannose-type glycans is an important feature in immunogen design, as glycans contribute to or influence the epitopes of numerous broadly neutralizing antibodies. Here we present a quantitative site-specific analysis of a recombinant, trimeric mimic of the native HIV-1 viral spike (BG505 SOSIP.664) compared to the corresponding uncleaved pseudotrimer and the matched gp120 monomer. We present a detailed molecular map of a trimer-associated glycan remodeling that forms a localized subdomain of the native mannose patch. The formation of native trimers is a critical design feature in shaping the glycan epitopes presented on recombinant vaccine candidates. IMPORTANCE: The envelope spike of human immunodeficiency virus type 1 (HIV-1) is a target for antibody-based neutralization. For some patients infected with HIV-1, highly potent antibodies have been isolated that can neutralize a wide range of circulating viruses. It is a goal of HIV-1 vaccine research to elicit these antibodies by immunization with recombinant mimics of the viral spike. These antibodies have evolved to recognize the dense array of glycans that coat the surface of the viral molecule. We show how the structure of these glycans is shaped by steric constraints imposed upon them by the native folding of the viral spike. This information is important in guiding the development of vaccine candidates.

Indexed as

Models, MolecularProtein ConformationProtein Multimerizationenv Gene Products, Human Immunodeficiency VirusGlycosylationHIV-1HumansMannosePolysaccharidesProtein BindingProteolysisStructure-Activity Relationshipenv Gene Products, Human Immunodeficiency VirusMannosePolysaccharidesfuringlycanglycosylationhuman immunodeficiency virusneutralizing antibodiesoligosaccharidesstructurevaccines

Identifiers

PMID27807235
PMCPMC5215339
OpenAlexW2546426623

What OpenQuestion holds

Textmetadata
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.