Evidence map›Paper›PMID 41298524›Full record

ArticleNature communications2025

Spatial constraints drive amylosome-mediated resistant starch degradation by Ruminococcus bromii in the human colon.

Benedikt H Wimmer, Sarah Moraïs, Itai Amit, Omar Tovar-Herrera, Meltem Tatli, Anke Trautwein-Schult, Barbara Pfister, Ran Zalk, Paloma Tödtli, Sebastian Simoni and 6 more

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Gut microbes · 2026
    Article
  2. Article
  3. Review
  4. Review
  5. Review
  6. Mucinolysome in gut microbiomes of farm animals and humans.bioRxiv : the preprint server for biology · 2025
    Article
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.

Benedikt H Wimmer *Department of Biochemistry, University of Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-6916-9360
Sarah Moraïs *Department of Life Sciences, Ben-Gurion-University of the Negev, Beer-Sheva, Israel.ORCID http://orcid.org/0000-0001-9026-2386
Itai AmitDepartment of Life Sciences, Ben-Gurion-University of the Negev, Beer-Sheva, Israel.
Omar Tovar-HerreraDepartment of Life Sciences, Ben-Gurion-University of the Negev, Beer-Sheva, Israel.ORCID http://orcid.org/0000-0001-7627-644X
Meltem TatliDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Anke Trautwein-SchultInstitute of Microbiology, Department of Microbial Proteomics, University of Greifswald, Greifswald, Germany.ORCID http://orcid.org/0000-0003-3272-5746
Barbara PfisterInstitute of Molecular Plant Biology, ETH Zurich, Zurich, Switzerland.ORCID http://orcid.org/0000-0002-4183-9625
Ran ZalkIlse Katz Institute for Nanoscale Science and Technology, Ben-Gurion University of the Negev, Beer-Sheva, Israel.ORCID http://orcid.org/0000-0003-4251-6497
Paloma TödtliDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Sebastian SimoniDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.
Matteo LisibachDepartment of Biochemistry, University of Zurich, Zurich, Switzerland.ORCID http://orcid.org/0009-0003-2351-5066
Liron LevinBioinformatics Core Facility, llse Katz Institute for Nanoscale Science and Technology, Ben-Gurion University of the Negev, Beer-Sheva, Israel.
Dörte BecherInstitute of Microbiology, Department of Microbial Proteomics, University of Greifswald, Greifswald, Germany.
Edward A BayerDepartment of Life Sciences, Ben-Gurion-University of the Negev, Beer-Sheva, Israel.ORCID http://orcid.org/0000-0001-7749-5150
Ohad MedaliaDepartment of Biochemistry, University of Zurich, Zurich, Switzerland. omedalia@bioc.uzh.ch.
Itzhak MizrahiDepartment of Life Sciences, Ben-Gurion-University of the Negev, Beer-Sheva, Israel. imizrahi@bgu.ac.il.ORCID http://orcid.org/0000-0001-6636-8818

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Degradation of complex dietary fiber by gut microbes is essential for colonic fermentation, short-chain fatty acid production, and microbiome function. Ruminococcus bromii is the primary resistant starch (RS) degrader in humans, which relies on the amylosome, a specialized cell-bound enzymatic complex. To unravel its architecture, function, and the interplay among its components, we applied a holistic multilayered approach: Cryo-electron tomography reveals that the amylosome comprises a constitutive extracellular layer extending toward the RS substrate. Proteomics demonstrates remodeling of its contents across different growth conditions, with Amy4 and Amy16 comprising 60% of the amylosome in response to RS. Structural and biochemical analyses reveal complementarity and synergistic RS degradation by these enzymes. We demonstrate that amylosome composition and RS degradation are regulated at two levels: structural constraints and expression-driven shifts in enzyme proportions enforce enzyme proximity, which allows R. bromii to fine-tune its adaptation to dietary fiber and shape colonic metabolism.

Indexed as

ColonRuminococcusStarchBacterial ProteinsCryoelectron MicroscopyDietary FiberGastrointestinal MicrobiomeHumansProteomicsBacterial ProteinsDietary FiberStarch

Identifiers

PMID41298524
PMCPMC12663171

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.