Title
Gramicidin A is hydrolyzed by a D-stereospecific peptidase produced by Bacillus anthracis
Author
Kaman, W.E.
Nazmi, K.
Voskamp-Visser, A.I.
Bikker, F.J.
Publication year
2022
Abstract
Previously we described the discovery of a Bacillus spp. specific peptidase activity related to Dstereospecific 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 DSPrelated 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.
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http://resolver.tudelft.nl/uuid:a395e126-2251-461c-8ae4-b36461a72804
DOI
https://doi.org/10.1111/1758-2229.13069
TNO identifier
967065
ISSN
1758-2229
Source
Environmental Microbiology Reports, 14 (14), 570-576
Document type
article