Gramicidin A is hydrolyzed by a d-stereospecific peptidase produced by Bacillus anthracis.
Journal
Environmental microbiology reports
ISSN: 1758-2229
Titre abrégé: Environ Microbiol Rep
Pays: United States
ID NLM: 101499207
Informations de publication
Date de publication:
08 2022
08 2022
Historique:
received:
31
03
2022
accepted:
02
04
2022
pubmed:
12
4
2022
medline:
27
7
2022
entrez:
11
4
2022
Statut:
ppublish
Résumé
Previously we described the discovery of a Bacillus spp. specific peptidase activity related to d-stereospecific peptidases (DSPs). The peptidase showed a strong preference for d-leucine and d-valine amino acids. These amino acids are present in the structure of the non-ribosomal peptide (NRP) antibiotics gramicidin A, B and C and polymyxin E. To examine if the Bacillus spp. DSP-related peptidase can hydrolyze these NRPs, the effect of gramicidin A and C and polymyxin E on peptidase activity in Bacillus anthracis culture supernatant was monitored. It was found that both gramicidins inhibited the DSP-related activity in a competitive manner. MALDI-TOF analysis revealed that upon incubation with B. anthracis culture supernatant gramicidin A hydrolyzation products appeared. This study shows that the Bacillus spp. specific DSP-like peptidase was potentially produced by the bacteria to gain intrinsic resistance against NRP antibiotics. These results are of utmost importance in research towards antimicrobial resistance, whereas transfer of DSP-related activity to other clinically relevant pathogens can be a serious threat to human health.
Identifiants
pubmed: 35403341
doi: 10.1111/1758-2229.13069
pmc: PMC9541196
doi:
Substances chimiques
Amino Acids
0
Anti-Bacterial Agents
0
Gramicidin
1405-97-6
Peptide Hydrolases
EC 3.4.-
Colistin
Z67X93HJG1
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
570-576Informations de copyright
© 2022 The Authors. Environmental Microbiology Reports published by Society for Applied Microbiology and John Wiley & Sons Ltd.
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