Acute melanization of silkworm hemolymph by peptidoglycans of the human commensal bacterium Cutibacterium acnes.
Journal
PloS one
ISSN: 1932-6203
Titre abrégé: PLoS One
Pays: United States
ID NLM: 101285081
Informations de publication
Date de publication:
2022
2022
Historique:
received:
29
06
2022
accepted:
12
09
2022
entrez:
26
9
2022
pubmed:
27
9
2022
medline:
28
9
2022
Statut:
epublish
Résumé
Cutibacterium acnes is a pathogenic bacterium that cause inflammatory diseases of the skin and intervertebral discs. The immune activation induced by C. acnes requires multiple cellular responses in the host. Silkworm, an invertebrate, generates melanin by phenoloxidase upon recognizing bacterial or fungal components. Therefore, the melanization reaction can be used as an indicator of innate immune activation. A silkworm infection model was developed for evaluating the virulence of C. acnes, but a system for evaluating the induction of innate immunity by C. acnes using melanization as an indicator has not yet been established. Here we demonstrated that C. acnes rapidly causes melanization of the silkworm hemolymph. On the other hand, Staphylococcus aureus, a gram-positive bacterium identical to C. acnes, does not cause immediate melanization. Even injection of heat-killed C. acnes cells caused melanization of the silkworm hemolymph. DNase, RNase, and protease treatment of the heat-treated C. acnes cells did not decrease the silkworm hemolymph melanization. Treatment with peptidoglycan-degrading enzymes, such as lysostaphin and lysozyme, however, decreased the induction of melanization by the heat-treated C. acnes cells. These findings suggest that silkworm hemolymph melanization may be a useful indicator to evaluate innate immune activation by C. acnes and that C. acnes peptidoglycans are involved in the induction of innate immunity in silkworms.
Identifiants
pubmed: 36155485
doi: 10.1371/journal.pone.0271420
pii: PONE-D-22-18420
pmc: PMC9512201
doi:
Substances chimiques
Melanins
0
Peptidoglycan
0
Monophenol Monooxygenase
EC 1.14.18.1
Deoxyribonucleases
EC 3.1.-
Ribonucleases
EC 3.1.-
Muramidase
EC 3.2.1.17
Lysostaphin
EC 3.4.24.75
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0271420Déclaration de conflit d'intérêts
The authors have declared that no competing interests exist.
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