Evidence map›Paper›PMID 35641660›Full record

ArticleCommunications biology2022

AA15 lytic polysaccharide monooxygenase is required for efficient chitinous cuticle turnover during insect molting.

Mingbo Qu, Xiaoxi Guo, Shuang Tian, Qing Yang, Myeongjin Kim, Seulgi Mun, Mi Young Noh, Karl J Kramer, Subbaratnam Muthukrishnan, Yasuyuki Arakane

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

12 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
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  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. The disordered C-terminal tail of fungal LPMOs from phytopathogens mediates protein dimerization and impacts plant penetration.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. Article
  12. Review
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 at 4 institutions in 3 countries.

Mingbo Qu *School of Bioengineering, Dalian University of Technology, 116024, Dalian, China.ORCID 0000-0003-0397-1630
Xiaoxi GuoSchool of Bioengineering, Dalian University of Technology, 116024, Dalian, China.
Shuang TianSchool of Bioengineering, Dalian University of Technology, 116024, Dalian, China.
Qing YangSchool of Bioengineering, Dalian University of Technology, 116024, Dalian, China. qingyang@dlut.edu.cn.ORCID 0000-0001-8623-7532
Myeongjin Kim *Department of Applied Biology, Chonnam National University, Gwangju, 61186, South Korea.
Seulgi MunDepartment of Applied Biology, Chonnam National University, Gwangju, 61186, South Korea.
Mi Young NohDepartment of Forest Resources, AgriBio Institute of Climate Change Management, Chonnam National University, Gwangju, 61186, South Korea.
Karl J KramerDepartment of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS, 66506, USA.
Subbaratnam MuthukrishnanDepartment of Biochemistry and Molecular Biophysics, Kansas State University, Manhattan, KS, 66506, USA.
Yasuyuki ArakaneDepartment of Applied Biology, Chonnam National University, Gwangju, 61186, South Korea. arakane@chonnam.ac.kr.ORCID 0000-0002-9538-1349
Chonnam National University · KRDalian University of Technology · CNKansas State University · USAgricultural Genomics Institute at Shenzhen · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microbial lytic polysaccharide monooxygenases (LPMOs) catalyze the oxidative cleavage of crystalline polysaccharides including chitin and cellulose. The discovery of a large assortment of LPMO-like proteins widely distributed in insect genomes suggests that they could be involved in assisting chitin degradation in the exoskeleton, tracheae and peritrophic matrix during development. However, the physiological functions of insect LPMO-like proteins are still undetermined. To investigate the functions of insect LPMO15 subgroup I-like proteins (LPMO15-1s), two evolutionarily distant species, Tribolium castaneum and Locusta migratoria, were chosen. Depletion by RNAi of T. castaneum TcLPMO15-1 caused molting arrest at all developmental stages, whereas depletion of the L. migratoria LmLPMO15-1, prevented only adult eclosion. In both species, LPMO15-1-deficient animals were unable to shed their exuviae and died. TEM analysis revealed failure of turnover of the chitinous cuticle, which is critical for completion of molting. Purified recombinant LPMO15-1-like protein from Ostrinia furnacalis (rOfLPMO15-1) exhibited oxidative cleavage activity and substrate preference for chitin. These results reveal the physiological importance of catalytically active LPMO15-1-like proteins from distant insect species and provide new insight into the enzymatic mechanism of cuticular chitin turnover during molting.

Indexed as

ChitinMixed Function OxygenasesAnimalsDietary CarbohydratesInsectaMoltingPolysaccharidesChitinDietary CarbohydratesMixed Function OxygenasesPolysaccharides

Identifiers

PMID35641660
PMCPMC9156745
OpenAlexW4281866259

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.