نتایج جستجو برای: shigella toxin b subunit stxb

تعداد نتایج: 1021086  

Journal: :The Journal of Experimental Medicine 1993
Y Lobet C Feron G Dequesne E Simoen P Hauser C Locht

Pertussis toxin plays a major role in the pathogenesis of whooping cough and is considered an important constituent of vaccines against this disease. It is composed of five different subunits associated in a molar ratio 1S1:1S2:1S3:2S4:1S5. The S1 subunit is responsible for the ADP-ribosyltransferase activity of the toxin. The B moiety, composed of S2 through S5, recognizes and binds to the tar...

Journal: :Molecular biology of the cell 2003
Yukako Fujinaga Anne A Wolf Chiara Rodighiero Heidi Wheeler Billy Tsai Larry Allen Michael G Jobling Tom Rapoport Randall K Holmes Wayne I Lencer

Cholera toxin (CT) travels from the plasma membrane of intestinal cells to the endoplasmic reticulum (ER) where a portion of the A-subunit, the A1 chain, crosses the membrane into the cytosol to cause disease. A related toxin, LTIIb, binds to intestinal cells but does not cause toxicity. Here, we show that the B-subunit of CT serves as a carrier for the A-subunit to the ER where disassembly occ...

2016
Kristien Velding Bert Mulder Jeroen Oeben Annelies Suurmeijer Thiemo F Veneman

Shigella toxin-producing Escherichia coli (STEC) is well known for its complications such as haemolytic uraemic syndrome (HUS), but neurological symptoms have also been reported. While most cases of infection with STEC occur with concurrent HUS, we describe a patient with severe neurological symptoms in the absence of HUS. LEARNING POINTS • Shigella toxin producing Escherichia coli (STEC) are b...

Journal: :Infection and immunity 1990
J T Barbieri M Pizza G Cortina R Rappuoli

degP-deficient strains of Escherichia coli grown in M-9 medium supplemented with ZnCl2 expressed the recombinant S1 subunit of pertussis toxin (rS1) in a form electrophoretically identical to the authentic S1 subunit. Subcellular fractionation showed that the full-length form of rS1 was membrane associated, while proteolytic fragments of rS1 were present in the periplasm. rS1 was extracted from...

Journal: :Journal of cell science 2004
Hisami Takenouchi Nobutaka Kiyokawa Tomoko Taguchi Jun Matsui Yohko U Katagiri Hajime Okita Kenji Okuda Junichiro Fujimoto

Shiga toxin is a bacterial toxin consisting of A and B subunits. Generally, the essential cytotoxicity of the toxin is thought to be mediated by the A subunit, which possesses RNA cleavage activity and thus induces protein synthesis inhibition. We previously reported, however, that the binding of the Shiga toxin 1-B subunit to globotriaosyl ceramide, a functional receptor for Shiga toxin, induc...

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