Differential Sensitivity of Human Epithelial Cells to Pseudomonas aeruginosa Exoenzyme S
نویسندگان
چکیده
منابع مشابه
Differential sensitivity of human epithelial cells to Pseudomonas aeruginosa exoenzyme S.
Exoenzyme S (ExoS) is an ADP-ribosyltransferase produced and directly translocated into eukaryotic cells by the opportunistic pathogen Pseudomonas aeruginosa. Model systems that allow bacterial translocation of ExoS have found ExoS to have multiple effects on eukaryotic cell function, affecting DNA synthesis, actin cytoskeletal structure, and cell matrix adherence. To understand mechanisms unde...
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Pseudomonas aeruginosa produces two distinct ADP-ribosyl transferases, exotoxin A and exoenzyme S, which differ in a number of properties including substrate specificity. Exoenzyme S was purified from culture supernatants of P. aeruginosa DG1. The procedure for purification consists of four major steps: ammonium sulfate precipitation, anion-exchange chromatography on DEAE-Sephacel, acetone prec...
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Exoenzyme S from Pseudomonas aeruginosa has been studied as an adhesion for glycosphingolipids and buccal cells. Binding of exoenzyme S to gangliotriosylceramide (GalNAc beta 1-4Gal beta 1-4Glc beta 1-1Cer), gangliotetraosylceramide (Gal beta 1-3 GalNAcT beta 1-4 Gal beta 1-4Glc beta 1-1Cer), and lactosylceramide (Gal beta 1-4Glc beta 1-1Cer) separated on thin-layer chromatograms was observed. ...
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Exoenzyme S (ExoS), an ADP-ribosylating enzyme produced by the opportunistic pathogen Pseudomonas aeruginosa, is directly translocated into eukaryotic cells by bacterial contact. Within the cell, ExoS ADP-ribosylates the cell signaling protein Ras and causes inhibition of DNA synthesis and alterations in cytoskeletal structure. To further understand the interrelationship of the different cellul...
متن کاملPurification and characterization of exoenzyme S from Pseudomonas aeruginosa 388.
Exoenzyme S was purified > 1,500-fold from the culture supernatant fluid of Pseudomonas aeruginosa 388 at high yield without utilization of solvents or detergents. Two proteins, with apparent molecular sizes of 53 and 49 kDa, cofractionated with exoenzyme S activity. Rabbit anti-49-kDa-protein immunoglobulin G was prepared by using sodium dodecyl sulfate-polyacrylamide gel electrophoresis-purif...
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ژورنال
عنوان ژورنال: Infection and Immunity
سال: 1999
ISSN: 0019-9567,1098-5522
DOI: 10.1128/iai.67.7.3494-3503.1999