Evidence map›Paper›PMID 33514845›Full record

ArticleCommunications biology2021

Post-correlation on-lamella cryo-CLEM reveals the membrane architecture of lamellar bodies.

Steffen Klein, Benedikt H Wimmer, Sophie L Winter, Androniki Kolovou, Vibor Laketa, Petr Chlanda

Open access · goldAbstract readVideo-Audio Media
In one paragraph

Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
7.6field-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

31 citing papers in PubMed, 53 citations in OpenAlex.

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  11. Recent advances in correlative cryo-light and electron microscopy.Current opinion in structural biology · 2024
    Review
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  14. Structure of the flotillin complex in a native membrane environment.Proceedings of the National Academy of Sciences of the United States of America · 2024
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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

6 authors at 1 institution in 1 country.

Steffen Klein *Schaller Research Groups, Department of Infectious Diseases-Virology, Heidelberg University, Heidelberg, Germany.ORCID 0000-0002-8046-0474
Benedikt H Wimmer *Schaller Research Groups, Department of Infectious Diseases-Virology, Heidelberg University, Heidelberg, Germany.
Sophie L WinterSchaller Research Groups, Department of Infectious Diseases-Virology, Heidelberg University, Heidelberg, Germany.
Androniki KolovouSchaller Research Groups, Department of Infectious Diseases-Virology, Heidelberg University, Heidelberg, Germany.
Vibor LaketaInfectious Diseases Imaging Platform (IDIP), Department of Infectious Diseases, Heidelberg University, Heidelberg, Germany.
Petr ChlandaSchaller Research Groups, Department of Infectious Diseases-Virology, Heidelberg University, Heidelberg, Germany. petr.chlanda@bioquant.uni-heidelberg.de.ORCID 0000-0002-7782-2139
Heidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lamellar bodies (LBs) are surfactant-rich organelles in alveolar cells. LBs disassemble into a lipid-protein network that reduces surface tension and facilitates gas exchange in the alveolar cavity. Current knowledge of LB architecture is predominantly based on electron microscopy studies using disruptive sample preparation methods. We established and validated a post-correlation on-lamella cryo-correlative light and electron microscopy approach for cryo-FIB milled cells to structurally characterize and validate the identity of LBs in their unperturbed state. Using deconvolution and 3D image registration, we were able to identify fluorescently labeled membrane structures analyzed by cryo-electron tomography. In situ cryo-electron tomography of A549 cells as well as primary Human Small Airway Epithelial Cells revealed that LBs are composed of membrane sheets frequently attached to the limiting membrane through "T"-junctions. We report a so far undescribed outer membrane dome protein complex (OMDP) on the limiting membrane of LBs. Our data suggest that LB biogenesis is driven by parallel membrane sheet import and by the curvature of the limiting membrane to maximize lipid storage capacity.

Indexed as

Cryoelectron MicroscopyElectron Microscope TomographyImage Interpretation, Computer-AssistedImaging, Three-DimensionalA549 CellsATP-Binding Cassette TransportersGreen Fluorescent ProteinsHumansIntracellular MembranesLung NeoplasmsOrganellesPulmonary AlveoliPulmonary Surfactant-Associated ProteinsRecombinant Fusion ProteinsABCA3 protein, humanATP-Binding Cassette Transportersenhanced green fluorescent proteinGreen Fluorescent ProteinsPulmonary Surfactant-Associated ProteinsRecombinant Fusion Proteins

Identifiers

PMID33514845
PMCPMC7846596
OpenAlexW3121535788

What OpenQuestion holds

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LicenceCC BY
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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.