نتایج جستجو برای: shigella toxin b subunit stxb

تعداد نتایج: 1021086  

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1982
G D Pearson J J Mekalanos

Hybridization probes derived from the A and B subunit genes of the heat-labile enterotoxin (LT) of Escherichia coli were used to analyze DNA from Vibrio cholera strain 569B for cholera toxin gene sequences. Southern blot analysis indicated that the cholera toxin A and B subunit genes were each duplicated in the strain. One of the two toxin subunit gene pairs was cloned as a 5.1-kilobase DNA ins...

Journal: :Journal of molecular biology 1995
R G Zhang D L Scott M L Westbrook S Nance B D Spangler G G Shipley E M Westbrook

The clinical manifestations of cholera are largely attributable to the actions of a secreted hexameric AB5 enterotoxin (choleragen). We have independently solved and refined the three-dimensional structure of choleragen at 2.5 A resolution. The structure of the crystalline toxin closely resembles that described for the heat-labile enterotoxin from Escherichia coli (LT) with which it shares 80% ...

Journal: :Infection and immunity 2012
Francisco J Martinez-Becerra Julian M Kissmann Jovita Diaz-McNair Shyamal P Choudhari Amy M Quick Gabriela Mellado-Sanchez John D Clements Marcela F Pasetti Wendy L Picking

Shigella spp. are food- and waterborne pathogens that cause severe diarrheal and dysenteric disease associated with high morbidity and mortality. Individuals most often affected are children under 5 years of age in the developing world. The existence of multiple Shigella serotypes and the heterogenic distribution of pathogenic strains, as well as emerging antibiotic resistance, require the deve...

Journal: :Infection and immunity 2004
Drusilla L Burns Stefanie Fiddner Anissa M Cheung Anita Verma

Pertussis toxin (PT) has an AB(5) structure that is typical of many bacterial protein toxins; however, this toxin is more complex than many toxins since it is composed of five different subunit types, subunits S1 to S5. Little is known about how PT assembles in vivo and how and when it interacts with its secretion apparatus, known as the Ptl transporter. In order to better understand these even...

2001
Wolfgang Lindner Frank A. Robey Charles R. Manclark

The relationship between the structure of the A subunit of pertussis toxin and its function was analyzed. Limited tryptic digestion of the A subunit converted the protein to two stable fragments (M. = 20,000 and 18,000). Antibodies raised to synthetic peptides homologous to regions in the A subunit were used to map these fragments. Both fragments were shown to contain the NHz-terminal portion b...

Journal: :Nucleic acids research 1983
M L Gennaro P J Greenaway

Nucleotide sequences coding for the N- and C-terminus of the A subunit and the N-terminus of the B subunit of cholera toxin were determined. These results show that the genes for the A and B subunits overlap out of phase by one nucleotide and that each subunit is synthesised as a precursor molecule which is subsequently processes after translation. It is proposed that the synthesis of each subu...

Journal: :Journal of cell science 2001
O Kovbasnjuk M Edidin M Donowitz

Enterohemorrhagic Escherichia coli producing Shiga toxins 1 and/or 2 have become major foodborne pathogens. The specific binding of Shiga toxin 1 B-subunit to its receptor, a neutral glycolipid globotriaosylceramide Gb(3), on the apical surface of colonic epithelium followed by toxin entry into cells are the initial steps of the process, which can result in toxin transcytosis and systemic effec...

Journal: :The Biochemical journal 1986
S L Griffiths R A Finkelstein D R Critchley

125I-labelled heat-labile toxin (from Escherichia coli) and 125I-labelled cholera toxin bound to immobilized ganglioside GM1 and Balb/c 3T3 cell membranes with identical specificities, i.e. each toxin inhibited binding of the other. Binding of both toxins to Balb/c 3T3 cell membranes was saturable, with 50% of maximal binding occurring at 0.3 nM for cholera toxin and 1.1 nM for heat-labile toxi...

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