نتایج جستجو برای: shigella toxin b subunit (stxb)

تعداد نتایج: 1021086  

Journal: :iranian journal of pharmaceutical sciences 0
hamid madanchi department of biology, imam houssein university, tehran, iran hossein honari department of biology, imam houssein university, tehran, iran mohammad sadraeian department of biology, imam houssein university, tehran, iran mahdi hesaraki department of biology, imam houssein university, tehran, iran

cholera toxin b subunit (ctxb) is a homopantameric, nontoxic subunit of cholera toxin that is responsible for its binding to the cell and has been known as a mucosal adjuvant for vaccines that could increase homoral and mocusal immunity response. in this work, the ctxb gene was fused to the stxb gene from shigella dysenteriae type i a vaccine antigen candidate against this pathogen, by a nonfur...

Background and Objective: Shiga toxin (STx) is the main virulence factor in Shigella Dysenteriae type I and is composed of an enzymatic subunit STxA monomer and a receptor-binding STxB homopentamer. Shigella toxin B subunit (STxB) is a non-toxic homopentameric protein responsible for toxin binding and internalization into target cells by interacting with glycolipid (Gb3). Cholera toxi...

املشی, ایمان, مینایی, محمد ابراهیم, هنری, حسین,

Background and purpose: The most common cause of diarrhea is Shigella and no vaccine has been found so far. IpaD and STxB proteins (B subunit of Shiga toxin) play an important role in invasion, infection and pathogenesis caused by Shigella. To evaluate the immunogenicity of each of the proteins IpaD and STxB can using of two animal models mice and guinea pigs and could be determined role of eac...

Hamid Madanchi Hossein Honari, Mahdi Hesaraki Mohammad Sadraeian

       Cholera toxin B subunit (CtxB) is a homopantameric, nontoxic subunit of cholera toxin that is responsible for its binding to the cell and has been known as a mucosal adjuvant for vaccines that could increase homoral and mocusal immunity response. In this work, the CtxB gene was fused to the StxB gene from Shigella dysenteriae type I a vaccine antigen candidate against t...

Journal: :Soft matter 2016
W Pezeshkian A G Hansen L Johannes H Khandelia J C Shillcock P B S Kumar J H Ipsen

The bacterial Shiga toxin is composed of an enzymatically active A-subunit, and a receptor-binding homopentameric B-subunit (STxB) that mediates intracellular toxin trafficking. Upon STxB-mediated binding to the glycolipid globotriaosylceramide (Gb3) at the plasma membrane of target cells, Shiga toxin is internalized by clathrin-dependent and independent endocytosis. The formation of tubular me...

Journal: :Biology of the cell 2006
Thomas Falguières Ludger Johannes

BACKGROUND INFORMATION In many cell lines, such as HeLa cells, STxB (Shiga toxin B-subunit) is transported from the plasma membrane to the ER (endoplasmic reticulum), via early/recycling endosomes and the Golgi apparatus, bypassing the late endocytic pathway. In human monocyte-derived macrophages and dendritic cells that are not sensitive to Shiga toxin-induced protein biosynthesis inhibition, ...

2009
Barbara Windschiegl Alexander Orth Winfried Römer Ludwig Berland Bahne Stechmann Patricia Bassereau Ludger Johannes Claudia Steinem

The homopentameric B-subunit of bacterial protein Shiga toxin (STxB) binds to the glycolipid Gb(3) in plasma membranes, which is the initial step for entering cells by a clathrin-independent mechanism. It has been suggested that protein clustering and lipid reorganization determine toxin uptake into cells. Here, we elucidated the molecular requirements for STxB induced Gb(3) clustering and for ...

Introduction: Shigella enterotoxin(STxB) is one of the major virulent factors in Shigella dysenteriae type 1 and E. coli O157:H7, which its immunogenicity, adjuvant and delivery characteristic have been proven. Anthrax is a common disease in humans and animals and identifies domain a-1 antibodies of protective antigen(PA) which is 62% of the PA antigens of Bacillus anthracis. Therefore, the pur...

Journal: :Infection and immunity 2007
Takeshi Shimizu Satomi Kawakami Toshio Sato Terumi Sasaki Masato Higashide Takashi Hamabata Toshiko Ohta Masatoshi Noda

Shiga toxins produced by enterohemorrhagic Escherichia coli (EHEC) include Shiga toxin 1 (Stx1) as well as Shiga toxin 2 (Stx2). Stx1 is cell associated, whereas Stx2 is localized to the culture supernatant. We have analyzed the secretion of Stx2 by generating histidine-tagged StxB (StxB-H). Although neither StxB1-H nor StxB2-H was secreted in StxB-H-overexpressed EHEC, StxB2-H-overexpressed EH...

Journal: :Molecular cancer therapeutics 2008
Thomas Falguières Matthias Maak Claus von Weyhern Marianne Sarr Xavier Sastre Marie-France Poupon Sylvie Robine Ludger Johannes Klaus-Peter Janssen

The targeting of solid tumors requires delivery tools that resist intracellular and extracellular inactivation, and that are taken up specifically by tumor cells. We have shown previously that the recombinant nontoxic B-subunit of Shiga toxin (STxB) can serve as a delivery tool to target digestive tumors in animal models. The aim of this study was to expand these experiments to human colorectal...

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