Contribution of Exoenzyme S to the Virulence of Pseudomonas aeruginosa1

2015 ◽  
pp. 40-48 ◽  
Author(s):  
Thalia I. Nicas ◽  
Barbara H. Iglewski
Keyword(s):  
Exoenzyme S

scholarly journals Structure–activity relationships for inhibitors of Pseudomonas aeruginosa exoenzyme S ADP-ribosyltransferase activity

2018 ◽  
Vol 143 ◽  
pp. 568-576 ◽  
Author(s):  
Michael Saleeb ◽  
Charlotta Sundin ◽  
Öznur Aglar ◽  
Ana Filipa Pinto ◽  
Mahsa Ebrahimi ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Exoenzyme S ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Adp Ribosyltransferase

The frequency of genes encoding exotoxin A and exoenzyme S in Pseudomonas aeruginosa strains isolated from burn patients

Burns ◽  
2016 ◽  
Vol 42 (5) ◽  
pp. 1116-1120 ◽  
Author(s):  
Azar Dokht Khosravi ◽  
Fatemeh Shafie ◽  
Effat Abbasi Montazeri ◽  
Soodabeh Rostami
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Burn Patients ◽  
Exotoxin A ◽  
Exoenzyme S ◽  
Genes Encoding

The Role of Exoenzyme S in Infections with Pseudomonas aeruginosa

1985 ◽  
Vol 152 (4) ◽  
pp. 716-721 ◽  
Author(s):  
T. I. Nicas ◽  
J. Bradley ◽  
J. E. Lochner ◽  
B. H. Iglewski
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Exoenzyme S

scholarly journals ADP-ribosylation of oncogenic Ras proteins by Pseudomonas aeruginosa exoenzyme S in vivo

1999 ◽  
Vol 32 (5) ◽  
pp. 1054-1064 ◽  
Author(s):  
Timothy S. Vincent ◽  
Jennifer E. Fraylick ◽  
Eileen M. McGuffie ◽  
Joan C. Olson
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Ras Proteins ◽  
Exoenzyme S ◽  
Adp Ribosylation ◽  
Oncogenic Ras

scholarly journals Pseudomonas aeruginosa Exoenzyme S Induces Transcriptional Expression of Proinflammatory Cytokines and Chemokines

2000 ◽  
Vol 68 (8) ◽  
pp. 4811-4814 ◽  
Author(s):  
Slava Epelman ◽  
Tony F. Bruno ◽  
Graham G. Neely ◽  
Donald E. Woods ◽  
Christopher H. Mody
Keyword(s):  
Cystic Fibrosis ◽  
Pseudomonas Aeruginosa ◽  
Proinflammatory Cytokines ◽  
Pulmonary Inflammation ◽  
Lung Damage ◽  
Gene Probe ◽  
Necrosis Factor Alpha ◽  
Exoenzyme S ◽  
Cytokines And Chemokines ◽  
Immunoregulatory Cytokines

ABSTRACT Pseudomonas aeruginosa infection of cystic fibrosis patients causes lung damage that is substantially orchestrated by cytokines. In this study, multi-gene probe analysis was used to characterize the ability of the P. aeruginosamitogen, exoenzyme S, to induce proinflammatory and immunoregulatory cytokines and chemokines. Exoenzyme S strongly induced transcription of proinflammatory cytokines and chemokines (tumor necrosis factor alpha, interleukin-1α [IL-1α], IL-1β, IL-6, IL-8, MIP-1α, MIP-1β, MCP-1, RANTES, and I-309), modest transcription of immunoregulatory cytokines (IL-10 and IL-12p40), and weak transcription of Th1 cytokines (IL-2 and gamma interferon). The response occurred early and subsided without evolving over time. These data suggest that cells responding to exoenzyme S would rapidly express proinflammatory cytokines and chemokines that may contribute to pulmonary inflammation in cystic fibrosis.

Exoenzyme S binds its cofactor 14-3-3 through a non-phosphorylated motif

2002 ◽  
Vol 30 (4) ◽  
pp. 401-405 ◽  
Author(s):  
B. Hallberg
Keyword(s):  
Specific Interaction ◽  
Phage Display Library ◽  
Bacterial Toxin ◽  
Inositol Polyphosphate ◽  
Checkpoint Control ◽  
Exoenzyme S ◽  
Infected Cells ◽  
Adp Ribosyltransferase

14-3-3 proteins belong to a family of conserved molecules, which play a regulatory role and participate in signal transduction and checkpoint control pathways. 14-3-3 proteins bind phosphoserine-phosphorylated ligands, such as the Raf-1 kinase and Bad, through recognition of the phosphorylated consensus motif, RSXpSXP (where pS is phosphoserine). Recently, a phosphorylation-independent interaction has been reported to occur between 14-3-3 and a small number of proteins, for example the 43 kDa inositol polyphosphate 5-phosphatase, glycoprotein Ib, p75NTR-associated cell-death executor (NADE) and the bacterial ADP-ribosyltransferase toxin exoenzyme S (ExoS). It has been suggested that specific residues of 14-3-3 proteins are required for activation of the bacterial toxin ExoS. An unphosphorylated peptide derived from a phage display library, known as the R18 peptide, and a synthetic peptide derived from ExoS inhibit the interaction between ExoS and 14-3-3. In this report we identify the amino acid sequence on ExoS which is responsible for its specific interaction with 14-3-3, both in vitro and in vivo. In addition, we believe that this interaction is critical for the ADP-ribosylation of an endogenous target, Ras, by ExoS both in vitro and in vivo. Loss of the 14-3-3-binding site on ExoS results in an ExoS molecule that is unable to efficiently inactivate Ras and shows a reduced capacity to change the morphology of infected cells, together with reduced killing activity.

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