Evidence map›Paper›PMID 38365249›Full record

ArticleThe ISME journal2024

Specialized digestive mechanism for an insect-bacterium gut symbiosis.

Junbeom Lee, Bohyun Jeong, Jeongtae Kim, Jae H Cho, Jin H Byeon, Bok L Lee, Jiyeun K Kim

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in The ISME journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Article
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 4 institutions in 4 countries.

Junbeom LeeMetabolomics Research Center for Functional Materials, Kyungsung University, Busan 48434, South Korea.
Bohyun JeongDepartment of Microbiology, Kosin University College of Medicine, Busan 49267, South Korea.
Jeongtae KimDepartment of Anatomy, Kosin University College of Medicine, Busan 49267, South Korea.
Jae H ChoHost Defense Protein Laboratory, College of Pharmacy, Pusan National University, Busan 46241, South Korea.
Jin H ByeonHost Defense Protein Laboratory, College of Pharmacy, Pusan National University, Busan 46241, South Korea.
Bok L LeeHost Defense Protein Laboratory, College of Pharmacy, Pusan National University, Busan 46241, South Korea.
Jiyeun K KimDepartment of Microbiology, Kosin University College of Medicine, Busan 49267, South Korea.
Kosin University · KRPusan National University · KRKyungsung University · KRNew Generation University College · ET

Funding

Ministry of Education RS-2023-00245952National Research Foundation of KoreaNRF Basic Science Research ProgramSouth Korean Government NRF-2021R1A2C1006793
6 · The paper itself

Abstract

In Burkholderia-Riptortus symbiosis, the host bean bug Riptortus pedestris harbors Burkholderia symbionts in its symbiotic organ, M4 midgut, for use as a nutrient source. After occupying M4, excess Burkholderia symbionts are moved to the M4B region, wherein they are effectively digested and absorbed. Previous studies have shown that M4B has strong symbiont-specific antibacterial activity, which is not because of the expression of antimicrobial peptides but rather because of the expression of digestive enzymes, mainly cathepsin L protease. However, in this study, inhibition of cathepsin L activity did not reduce the bactericidal activity of M4B, indicating that there is an unknown digestive mechanism that renders specifically potent bactericidal activity against Burkholderia symbionts. Transmission electron microscopy revealed that the lumen of symbiotic M4B was filled with a fibrillar matter in contrast to the empty lumen of aposymbiotic M4B. Using chromatographic and electrophoretic analyses, we found that the bactericidal substances in M4B existed as high-molecular-weight (HMW) complexes that were resistant to protease degradation. The bactericidal HMW complexes were visualized on non-denaturing gels using protein- and polysaccharide-staining reagents, thereby indicating that the HMW complexes are composed of proteins and polysaccharides. Strongly stained M4B lumen with Periodic acid-Schiff (PAS) reagent in M4B paraffin sections confirmed HMW complexes with polysaccharide components. Furthermore, M4B smears stained with Periodic acid-Schiff revealed the presence of polysaccharide fibers. Therefore, we propose a key digestive mechanism of M4B: bacteriolytic fibers, polysaccharide fibers associated with digestive enzymes such as cathepsin L, specialized for Burkholderia symbionts in Riptortus gut symbiosis.

Indexed as

BurkholderiaHeteropteraAnimalsBacteriaCathepsin LInsectaPeriodic AcidPolysaccharidesSymbiosisCathepsin LPeriodic AcidPolysaccharidesBurkholderiafibersmidgutRiptortus pedestrissymbiosis

Identifiers

PMID38365249
PMCPMC10811733
OpenAlexW4390704145

What OpenQuestion holds

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LicenceCC BY
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.