Evidence map›Paper›PMID 26283800›Full record

ArticleThe Journal of cell biology2015

Live-cell observation of cytosolic HIV-1 assembly onset reveals RNA-interacting Gag oligomers.

Jelle Hendrix, Viola Baumgärtel, Waldemar Schrimpf, Sergey Ivanchenko, Michelle A Digman, Enrico Gratton, Hans-Georg Kräusslich, Barbara Müller, Don C Lamb

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

69 citing papers in PubMed, 102 citations in OpenAlex.

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  6. Membrane bending energy selects for compact growth of protein assemblies.bioRxiv : the preprint server for biology · 2025
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  17. Atomic view of the HIV-1 matrix lattice; implications on virus assembly and envelope incorporation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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9 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 7 institutions in 2 countries.

Jelle HendrixPhysical Chemistry, Department of Chemistry, Ludwig Maximilian University of Munich, D-81377 Munich, Germany NanoSystems Initiative Munich (NIM), Ludwig Maximilian University of Munich, D-81377 Munich, Germany Munich Center for Integrated Protein Science (CiPSM), Ludwig Maximilian University of Munich, D-81377 Munich, Germany Center for Nanoscience (CeNS), Ludwig Maximilian University of Munich, D-81377 Munich, Germany.
Viola BaumgärtelPhysical Chemistry, Department of Chemistry, Ludwig Maximilian University of Munich, D-81377 Munich, Germany NanoSystems Initiative Munich (NIM), Ludwig Maximilian University of Munich, D-81377 Munich, Germany Munich Center for Integrated Protein Science (CiPSM), Ludwig Maximilian University of Munich, D-81377 Munich, Germany Center for Nanoscience (CeNS), Ludwig Maximilian University of Munich, D-81377 Munich, Germany.
Waldemar SchrimpfPhysical Chemistry, Department of Chemistry, Ludwig Maximilian University of Munich, D-81377 Munich, Germany NanoSystems Initiative Munich (NIM), Ludwig Maximilian University of Munich, D-81377 Munich, Germany Munich Center for Integrated Protein Science (CiPSM), Ludwig Maximilian University of Munich, D-81377 Munich, Germany Center for Nanoscience (CeNS), Ludwig Maximilian University of Munich, D-81377 Munich, Germany.
Sergey IvanchenkoPhysical Chemistry, Department of Chemistry, Ludwig Maximilian University of Munich, D-81377 Munich, Germany NanoSystems Initiative Munich (NIM), Ludwig Maximilian University of Munich, D-81377 Munich, Germany Munich Center for Integrated Protein Science (CiPSM), Ludwig Maximilian University of Munich, D-81377 Munich, Germany Center for Nanoscience (CeNS), Ludwig Maximilian University of Munich, D-81377 Munich, Germany.
Michelle A DigmanLaboratory for Fluorescence Dynamics, Department of Biomedical Engineering, University of California, Irvine, Irvine, CA 92697 Development Biology Center Optical Biology Core Facility, University of California, Irvine, Irvine, CA 92697.
Enrico GrattonLaboratory for Fluorescence Dynamics, Department of Biomedical Engineering, University of California, Irvine, Irvine, CA 92697 Development Biology Center Optical Biology Core Facility, University of California, Irvine, Irvine, CA 92697.
Hans-Georg KräusslichDepartment of Infectious Diseases, Virology, University Hospital Heidelberg, D-69120 Heidelberg, Germany.
Barbara MüllerDepartment of Infectious Diseases, Virology, University Hospital Heidelberg, D-69120 Heidelberg, Germany.
Don C LambPhysical Chemistry, Department of Chemistry, Ludwig Maximilian University of Munich, D-81377 Munich, Germany NanoSystems Initiative Munich (NIM), Ludwig Maximilian University of Munich, D-81377 Munich, Germany Munich Center for Integrated Protein Science (CiPSM), Ludwig Maximilian University of Munich, D-81377 Munich, Germany Center for Nanoscience (CeNS), Ludwig Maximilian University of Munich, D-81377 Munich, Germany d.lamb@lmu.de.
Center for Integrated Protein Science Munich · DECenter for NanoScience · DEFluor (United States) · USHeidelberg University · DELudwig-Maximilians-Universität München · DEUniversity Hospital Heidelberg · DEUniversity of California, Irvine · US

Funding

Uncover Strategies Used By Biological SystemsP50GM076516 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI NIE, QING · 2007 to 2016
$25.1M
TRD4: Phasor analysisP41GM103540 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI GRATTON, ENRICO · 2012 to 2020
$12.5M
NIGMS NIH HHS P41 GM103540NIGMS NIH HHS P50 GM076516NIGMS NIH HHS P50-GM076516
6 · The paper itself

Abstract

Assembly of the Gag polyprotein into new viral particles in infected cells is a crucial step in the retroviral replication cycle. Currently, little is known about the onset of assembly in the cytosol. In this paper, we analyzed the cytosolic HIV-1 Gag fraction in real time in live cells using advanced fluctuation imaging methods and thereby provide detailed insights into the complex relationship between cytosolic Gag mobility, stoichiometry, and interactions. We show that Gag diffuses as a monomer on the subsecond timescale with severely reduced mobility. Reduction of mobility is associated with basic residues in its nucleocapsid (NC) domain, whereas capsid (CA) and matrix (MA) domains do not contribute significantly. Strikingly, another diffusive Gag species was observed on the seconds timescale that oligomerized in a concentration-dependent manner. Both NC- and CA-mediated interactions strongly assist this process. Our results reveal potential nucleation steps of cytosolic Gag fractions before membrane-assisted Gag assembly.

Indexed as

Virus AssemblyAmino Acid SequenceCytoplasmgag Gene Products, Human Immunodeficiency VirusHeLa CellsHIV-1HumansMolecular Sequence DataProtein MultimerizationProtein TransportSingle-Cell Analysisgag Gene Products, Human Immunodeficiency Virus

Identifiers

PMID26283800
PMCPMC4539982
OpenAlexW2115221527

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.