Evidence map›Paper›PMID 30936472›Full record

ArticleNature cell biology2019

A lipid-based partitioning mechanism for selective incorporation of proteins into membranes of HIV particles.

Prabuddha Sengupta, Arnold Y Seo, H Amalia Pasolli, Yul Eum Song, Marc C Johnson, Jennifer Lippincott-Schwartz

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Nature cell biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
6.8field-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

75 citing papers in PubMed, 124 citations in OpenAlex.

  1. Mechanisms of HIV-1 assembly, release and maturation.Nature reviews. Microbiology · 2026
    Review
  2. Devising a divisome for synthetic cells.Nature reviews. Chemistry · 2026
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. PIPScience advances · 2025
    Article
  13. Article
  14. HIV-1 budding requires cortical actin disassembly by the oxidoreductase MICAL1.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Article
  16. Article
  17. Cooperative Membrane Binding of HIV-1 Matrix Proteins.The journal of physical chemistry. B · 2024
    Article
  18. Article
  19. Article
  20. Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 1 country.

Prabuddha SenguptaHoward Hughes Medical Institute, Janelia Research Campus, Ashburn, VA, USA. senguptap@janelia.hhmi.org.ORCID http://orcid.org/0000-0001-7094-6967
Arnold Y SeoHoward Hughes Medical Institute, Janelia Research Campus, Ashburn, VA, USA.
H Amalia PasolliHoward Hughes Medical Institute, Janelia Research Campus, Ashburn, VA, USA.
Yul Eum SongDepartment of Molecular Microbiology and Immunology, Christopher S. Bond Life Sciences Center, University of Missouri, Columbia, MO, USA.
Marc C JohnsonDepartment of Molecular Microbiology and Immunology, Christopher S. Bond Life Sciences Center, University of Missouri, Columbia, MO, USA.
Jennifer Lippincott-SchwartzHoward Hughes Medical Institute, Janelia Research Campus, Ashburn, VA, USA. lippincottschwartzj@janelia.hhmi.org.ORCID http://orcid.org/0000-0002-8601-3501
Howard Hughes Medical Institute · USUniversity of Missouri · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Particles that bud off from the cell surface, including viruses and microvesicles, typically have a unique membrane protein composition distinct from that of the originating plasma membrane. This selective protein composition enables viruses to evade the immune response and infect other cells. But how membrane proteins sort into budding viruses such as human immunodeficiency virus (HIV) remains unclear. Proteins could passively distribute into HIV-assembly-site membranes producing compositions resembling pre-existing plasma-membrane domains. Here, we demonstrate that proteins instead sort actively into HIV-assembly-site membranes, generating compositions enriched in cholesterol and sphingolipids that undergo continuous remodelling. Proteins are recruited into and removed from the HIV assembly site through lipid-based partitioning, initiated by oligomerization of the HIV structural protein Gag. Changes in membrane curvature at the assembly site further amplify this sorting process. Thus, a lipid-based sorting mechanism, aided by increasing membrane curvature, generates the unique membrane composition of the HIV surface.

Indexed as

AnimalsBone Marrow Stromal Antigen 2Cell MembraneChlorocebus aethiopsCOS CellsEndosomal Sorting Complexes Required for TransportHeLa CellsHIVHuman Immunodeficiency Virus ProteinsHumansMembrane LipidsMembrane ProteinsVirionBone Marrow Stromal Antigen 2Endosomal Sorting Complexes Required for TransportHuman Immunodeficiency Virus ProteinsMembrane LipidsMembrane Proteins

Identifiers

PMID30936472
OpenAlexW2926355223

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.