Evidence map›Paper›PMID 39438475›Full record

ArticleScientific reports2024

Molecular identification of hyaluronate lyase, not hyaluronidase, as an intrinsic hyaluronan-degrading enzyme in Clostridium perfringens strain ATCC 13124.

Tomoya Kumon, Sayoko Oiki, Wataru Hashimoto

Abstract read
In one paragraph

Article in Scientific reports, 2024. 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. Article
  2. Review
  3. Characterization ofInfection and drug resistance · 2026
    Article
  4. Review
  5. Article
  6. Hyaluronidases improve the hyaluronic acid yield during the fermentation ofFrontiers in bioengineering and biotechnology · 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

3 authors.

Tomoya Kumon *Laboratory of Basic and Applied Molecular Biotechnology, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Kyoto, 611-0011, Japan.
Sayoko Oiki *Laboratory of Basic and Applied Molecular Biotechnology, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Kyoto, 611-0011, Japan.
Wataru HashimotoLaboratory of Basic and Applied Molecular Biotechnology, Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Kyoto, 611-0011, Japan. hashimoto.wataru.8c@kyoto-u.ac.jp.

Funding

Japan Society for the Promotion of Science 15H04629
6 · The paper itself

Abstract

Clostridium perfringens, an opportunistic pathogen, produces mu-toxin hyaluronidases including endo-β-N-acetylglucosaminidases (Nags) as a virulence invasion factor. To clarify an intrinsic factor for degradation of host extracellular hyaluronan, we focused on hyaluronate lyase (HysA), distinct from endo-β-N-acetylglucosaminidases. C. perfringens strain ATCC 13124 was found to assimilate host-derived extracellular mucosubstances, hyaluronan and mucin, which induced expression of the hyaluronan-related genetic cluster, including hyaluronate lyase gene (hysA), but repressed endo-β-N-acetylglucosaminidase genes. This genetic cluster is conserved in some strains of C. perfringens. The recombinant strain ATCC 13124 hyaluronate lyase HysA showed an hyaluronan-degrading activity through β-elimination reaction. The hyaluronan-degrading enzyme in the culture supernatant of strain ATCC 13124 exhibited the lyase activity and was identical to the recombinant hyaluronate lyase on the native-PAGE gel, followed by activity straining. These results demonstrated that the intrinsic hyaluronan-degrading enzyme of C. perfringens strain ATCC 13124 is hyaluronate lyase HysA, but not hyaluronidases NagH, NagJ, and NagK.

Indexed as

Clostridium perfringensHyaluronic AcidPolysaccharide-LyasesBacterial ProteinsHyaluronoglucosaminidaseMultigene FamilyBacterial Proteinshyaluronate lyaseHyaluronic AcidHyaluronoglucosaminidasePolysaccharide-Lyases

Identifiers

PMID39438475
PMCPMC11496695

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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.