Molecular identification of hyaluronate lyase, not hyaluronidase, as an intrinsic hyaluronan-degrading enzyme in Clostridium perfringens strain ATCC 13124.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
22 10 2024
22 10 2024
Historique:
received:
23
04
2024
accepted:
23
09
2024
medline:
23
10
2024
pubmed:
23
10
2024
entrez:
22
10
2024
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 39438475
doi: 10.1038/s41598-024-73955-y
pii: 10.1038/s41598-024-73955-y
doi:
Substances chimiques
hyaluronate lyase
EC 4.2.2.1
Polysaccharide-Lyases
EC 4.2.2.-
Hyaluronic Acid
9004-61-9
Bacterial Proteins
0
Hyaluronoglucosaminidase
EC 3.2.1.35
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
24266Subventions
Organisme : Japan Society for the Promotion of Science
ID : 15H04629
Informations de copyright
© 2024. The Author(s).
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