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פותח על ידי קלירמאש פתרונות בע"מ -
Direct Binding of Salicylic Acid to PectobacteriumN-Acyl-Homoserine Lactone Synthase
Year:
2020
Source of publication :
ACS chemical biology
Authors :
ג'ושי, ג'נאק ראג'
;
.
ידידיה, איריס
;
.
כרמי, ניר
;
.
Volume :
15
Co-Authors:

Joshi, J.R.- Department of Plant Pathology and Microbiology, Hebrew University of Jerusalem, Rehovot, 76100, Israel; Department of Plant Sciences, Agricultural Research Organization, Volcani Center, Israel. 
Khazanov, N.- Department of Chemistry, Ramat-Gan 5290002, Bar-Ilan University, Israel.  
Khadka, N.- Department of Plant Pathology and Microbiology, Hebrew University of Jerusalem, Rehovot, 76100, Israel; Department of Plant Sciences, Agricultural Research Organization, Volcani Center, Israel. 
 
Charkowski, A.O. - Department of Agricultural Biology, Colorado State University, Fort Collins, CO 80523, United States.

Burdman, S.- Department of Plant Pathology and Microbiology, Hebrew University of Jerusalem, Rehovot, 76100, Israel. 
Senderowitz, H. - Department of Chemistry, Ramat-Gan 5290002, Bar-Ilan University, Israel

Facilitators :
From page:
0
To page:
0
(
Total pages:
1
)
Abstract:

Salicylic acid (SA) is a hormone that mediates systemic acquired resistance in plants. We demonstrated that SA can interfere with group behavior and virulence of the soft-rot plant pathogen Pectobacterium spp. through quorum sensing (QS) inhibition. QS is a population density-dependent communication system that relies on the signal molecule acyl-homoserine lactone (AHL) to synchronize infection. P. parmentieri mutants, lacking the QS AHL synthase (expI-) or the response regulator (expR-), were used to determine how SA inhibits QS. ExpI was expressed in DH5α, the QS negative strain of Escherichia coli, revealing direct interference of SA with AHL synthesis. Docking simulations showed SA is a potential ExpI ligand. This hypothesis was further confirmed by direct binding of SA to purified ExpI, shown by isothermal titration calorimetry and microscale thermophoresis. Computational alanine scanning was employed to design a mutant ExpI with predicted weaker binding affinity to SA. The mutant was constructed and displayed lower affinity to the ligand in the binding assay, and its physiological inhibition by SA was reduced. Taken together, these data support a likely mode of action and a role for SA as potent inhibitor of AHL synthase and QS.

Note:
Related Files :
Acyl-Butyrolactones
N-octanoylhomoserine lactone
Pectobacterium spp.
quorum sensing
Salicylic acid
עוד תגיות
תוכן קשור
More details
DOI :
10.1021/acschembio.0c00185
Article number:
0
Affiliations:
Database:
סקופוס
Publication Type:
מאמר
;
.
Language:
אנגלית
Editors' remarks:
ID:
48838
Last updated date:
02/03/2022 17:27
Creation date:
05/08/2020 17:36
You may also be interested in
Scientific Publication
Direct Binding of Salicylic Acid to PectobacteriumN-Acyl-Homoserine Lactone Synthase
15

Joshi, J.R.- Department of Plant Pathology and Microbiology, Hebrew University of Jerusalem, Rehovot, 76100, Israel; Department of Plant Sciences, Agricultural Research Organization, Volcani Center, Israel. 
Khazanov, N.- Department of Chemistry, Ramat-Gan 5290002, Bar-Ilan University, Israel.  
Khadka, N.- Department of Plant Pathology and Microbiology, Hebrew University of Jerusalem, Rehovot, 76100, Israel; Department of Plant Sciences, Agricultural Research Organization, Volcani Center, Israel. 
 
Charkowski, A.O. - Department of Agricultural Biology, Colorado State University, Fort Collins, CO 80523, United States.

Burdman, S.- Department of Plant Pathology and Microbiology, Hebrew University of Jerusalem, Rehovot, 76100, Israel. 
Senderowitz, H. - Department of Chemistry, Ramat-Gan 5290002, Bar-Ilan University, Israel

Direct Binding of Salicylic Acid to PectobacteriumN-Acyl-Homoserine Lactone Synthase

Salicylic acid (SA) is a hormone that mediates systemic acquired resistance in plants. We demonstrated that SA can interfere with group behavior and virulence of the soft-rot plant pathogen Pectobacterium spp. through quorum sensing (QS) inhibition. QS is a population density-dependent communication system that relies on the signal molecule acyl-homoserine lactone (AHL) to synchronize infection. P. parmentieri mutants, lacking the QS AHL synthase (expI-) or the response regulator (expR-), were used to determine how SA inhibits QS. ExpI was expressed in DH5α, the QS negative strain of Escherichia coli, revealing direct interference of SA with AHL synthesis. Docking simulations showed SA is a potential ExpI ligand. This hypothesis was further confirmed by direct binding of SA to purified ExpI, shown by isothermal titration calorimetry and microscale thermophoresis. Computational alanine scanning was employed to design a mutant ExpI with predicted weaker binding affinity to SA. The mutant was constructed and displayed lower affinity to the ligand in the binding assay, and its physiological inhibition by SA was reduced. Taken together, these data support a likely mode of action and a role for SA as potent inhibitor of AHL synthase and QS.

Scientific Publication
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