Evidence map›Paper›PMID 40401997›Full record

ArticleThe ISME journal2025

Complete xylan utilization pathway and regulation mechanisms involved in marine algae degradation by cosmopolitan marine and human gut microbiota.

Hai-Ning Sun, Xiu-Lan Chen, Yan Wang, Yan-Ping Zhu, Zhao-Jie Teng, Hai-Yan Cao, Ting-Ting Xu, Yin Chen, Yu-Zhong Zhang, Fang Zhao

Abstract read
In one paragraph

Article in The ISME journal, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

10 authors.

Hai-Ning SunState Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, Shandong Province, China.
Xiu-Lan ChenState Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, Shandong Province, China.
Yan WangState Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, Shandong Province, China.
Yan-Ping ZhuState Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, Shandong Province, China.
Zhao-Jie TengState Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, Shandong Province, China.
Hai-Yan CaoState Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, Shandong Province, China.
Ting-Ting XuState Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, Shandong Province, China.
Yin ChenMOE Key Laboratory of Evolution and Marine Biodiversity, Frontiers Science Center for Deep Ocean Multispheres and Earth System & College of Marine Life Sciences, Ocean University of China, Qingdao 266003, Shandong Province, China.
Yu-Zhong ZhangMOE Key Laboratory of Evolution and Marine Biodiversity, Frontiers Science Center for Deep Ocean Multispheres and Earth System & College of Marine Life Sciences, Ocean University of China, Qingdao 266003, Shandong Province, China.
Fang ZhaoState Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, Shandong Province, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

β-1,3-xylan, typically found in marine algae as a major cell wall polysaccharide, represents an overlooked pool of organic carbon in global oceans. Whilst our understanding of microbial catabolism of xylans has improved significantly, particularly from biotransformations of terrestrial plant biomass that are typically composed of β-1,4-xylans, knowledge on how microbes utilize β-1,3-xylan remains limited. Here, we describe the discovery of a complete pathway for β-1,3-xylan catabolism and its regulation in a marine bacterium, Vibrio sp. EA2. The pathway starts with the extracellular decomposition of β-1,3-xylan by two β-1,3-xylanases into β-1,3-xylooligomers, which are mainly internalized by an ATP-binding cassette transporter. The substrate binding protein of this transporter has an L-shaped substrate binding pocket to preferentially bind β-1,3-xylooligomers. Subsequently, two intracellular β-1,3-xylosidases degrade β-1,3-xylooligomers into fermentable xylose. The pathway is activated by a unique regulator with xylose being the effector. This β-1,3-xylan catabolic pathway differs from that of β-1,4-xylan catabolism in enzymes, transporters, and regulators. Bioinformatic analysis suggests that the β-1,3-xylan catabolism pathway is not only prevalent in diverse marine bacteria and cosmopolitan human gut microbiota, such as Bacteroides, but also likely transferred horizontally from algae-degrading marine bacteria to the human gut.

Indexed as

Gastrointestinal MicrobiomeMetabolic Networks and PathwaysVibrioXylansHumansSeawaterXylanscatabolism pathwayhuman gut microbiotamarine algaemarine bacteriaβ-1,3-xylan

Identifiers

PMID40401997
PMCPMC12125979

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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.