Evidence map›Paper›PMID 39738071›Full record

ArticleNature communications2024

Mechanisms of recalcitrant fucoidan breakdown in marine Planctomycetota.

Carla Pérez-Cruz, Alicia Moraleda-Montoya, Raquel Liébana, Oihana Terrones, Uxue Arrizabalaga, Mikel García-Alija, Maier Lorizate, Ana Martínez Gascueña, Isabel García-Álvarez, Jon Ander Nieto-Garai and 8 more

Abstract read
In one paragraph

Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Review
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  16. Structural insights into a fucosidase involved in fucoidan degradation.Acta crystallographica. Section F, Structural biology communications · 2025
    Article
  17. Article
  18. Article
  19. Review
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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

18 authors.

Carla Pérez-Cruz *AZTI, Marine Research, Basque Research and Technology Alliance (BRTA), Sukarrieta, Spain.
Alicia Moraleda-Montoya *Structural Glycoimmunology Laboratory, Biobizkaia Health Research Institute, Barakaldo, Spain.
Raquel Liébana *AZTI, Marine Research, Basque Research and Technology Alliance (BRTA), Sukarrieta, Spain.
Oihana TerronesDepartment of Biochemistry and Molecular Biology, Faculty of Science and Technology, University of the Basque Country, Leioa, Spain.
Uxue ArrizabalagaAZTI, Marine Research, Basque Research and Technology Alliance (BRTA), Sukarrieta, Spain.
Mikel García-AlijaStructural Glycoimmunology Laboratory, Biobizkaia Health Research Institute, Barakaldo, Spain.
Maier LorizateDepartment of Biochemistry and Molecular Biology, Faculty of Science and Technology, University of the Basque Country, Leioa, Spain.
Ana Martínez GascueñaStructural Glycoimmunology Laboratory, Biobizkaia Health Research Institute, Barakaldo, Spain.
Isabel García-ÁlvarezFacultad de Ciencias Experimentales, Universidad Francisco de Vitoria, Pozuelo de Alarcón, Madrid, Spain.ORCID 0000-0002-2273-5046
Jon Ander Nieto-GaraiDepartment of Biochemistry and Molecular Biology, Faculty of Science and Technology, University of the Basque Country, Leioa, Spain.ORCID 0000-0002-8665-099X
June Olazar-IntxaustiDepartment of Biochemistry and Molecular Biology, Faculty of Science and Technology, University of the Basque Country, Leioa, Spain.
Bárbara Rodríguez-ColinasFacultad de Ciencias Experimentales, Universidad Francisco de Vitoria, Pozuelo de Alarcón, Madrid, Spain.
Enrique MannInstituto de Química Orgánica General (IQOG-CSIC), Madrid, Spain.
José Luis ChiaraInstituto de Química Orgánica General (IQOG-CSIC), Madrid, Spain.ORCID 0000-0002-8153-1852
Francesc-Xabier ContrerasDepartment of Biochemistry and Molecular Biology, Faculty of Science and Technology, University of the Basque Country, Leioa, Spain. xabier.contreras@ehu.eus.ORCID 0000-0003-0875-634X
Marcelo E GuerinStructural Glycobiology Laboratory, Department of Structural and Molecular Biology; Molecular Biology Institute of Barcelona (IBMB), Spanish National Research Council (CSIC), Barcelona Science Park, Tower R, Barcelona, Spain. mrccri@ibmb.csic.es.ORCID 0000-0001-9524-3184
Beatriz TrastoyStructural Glycoimmunology Laboratory, Biobizkaia Health Research Institute, Barakaldo, Spain. beatriz.trastoy@gmail.com.ORCID 0000-0002-2178-732X
Laura Alonso-SáezAZTI, Marine Research, Basque Research and Technology Alliance (BRTA), Sukarrieta, Spain. lalonso@azti.es.ORCID 0000-0003-1757-4767

Funding

Rationalizing glycoengineering strategies for immunotherapeutic antibodiesR01AI149297 · NIAID · EMORY UNIVERSITY · PI JEFFREY Victor RAVETCH, ERIC JOHN SUNDBERG · 2020 to 2026
$3.7M
Eusko Jaurlaritza (Basque Government) BIOMATRIXEusko Jaurlaritza (Basque Government) KK-2021-00034Eusko Jaurlaritza (Basque Government) KK-2022/00107Ministerio de Economía y Competitividad (Ministry of Economy and Competitiveness) PID2019-105649RB-I00Ministerio de Economía y Competitividad (Ministry of Economy and Competitiveness) PID2020-117405GB100Ministerio de Economía y Competitividad (Ministry of Economy and Competitiveness) PID2021-122177NA-I00Ministerio de Economía y Competitividad (Ministry of Economy and Competitiveness) PID2021-125469NB-C33NIAID NIH HHS R01 AI149297
6 · The paper itself

Abstract

Marine brown algae produce the highly recalcitrant polysaccharide fucoidan, contributing to long-term oceanic carbon storage and climate regulation. Fucoidan is degraded by specialized heterotrophic bacteria, which promote ecosystem function and global carbon turnover using largely uncharacterized mechanisms. Here, we isolate and study two Planctomycetota strains from the microbiome associated with the alga Fucus spiralis, which grow efficiently on chemically diverse fucoidans. One of the strains appears to internalize the polymer, while the other strain degrades it extracellularly. Multi-omic approaches show that fucoidan breakdown is mediated by the expression of divergent polysaccharide utilization loci, and endo-fucanases of family GH168 are strongly upregulated during fucoidan digestion. Enzymatic assays and structural biology studies reveal how GH168 endo-fucanases degrade various fucoidan cores from brown algae, assisted by auxiliary hydrolytic enzymes. Overall, our results provide insights into fucoidan processing mechanisms in macroalgal-associated bacteria.

Indexed as

FucusPolysaccharidesAquatic OrganismsBacteriaGlycoside HydrolasesMicrobiotaPhylogenyfucoidanGlycoside HydrolasesPolysaccharides

Identifiers

PMID39738071
PMCPMC11685898

What OpenQuestion holds

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LicenceCC BY-NC-ND
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Registered trials

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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.