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Shiga toxin (Stx) ribosomal interactions
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Abyad, Jenna Tawil. Shiga toxin (Stx) ribosomal interactions. Retrieved from https://doi.org/doi:10.7282/t3-j8h6-z233

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TitleShiga toxin (Stx) ribosomal interactions
NameAbyad, Jenna Tawil (author); Tumer, Nilgun (chair); Kahn, Peter (member); Haimovich, Beatrice (member); Langer, Jerome (member); Rutgers University; School of Graduate Studies
Date Created2021
Other Date2021-10 (degree)
SubjectMicrobiology, Biochemistry, Verocytotoxins, A1 subunit, Ribosomal interactions, Shiga toxin
Extent1 online resource (v, 20 pages) : illustrations
DescriptionInfection by foodborne pathogens such as Shiga toxin producing E. coli (STEC) and Shigella dysenteriae can lead to the development of either hemorrhagic colitis (HC) or hemolytic uremic syndrome (HUS), which can be fatal. Shiga toxins (Stxs) produced by these bacteria are virulence factors that can attack the blood vessels in the kidneys, causing HUS, which is the leading cause of renal failure in young children. Stxs are AB5 toxins composed of an enzymatically active A1 subunit and five copies of a B subunit. The A1 subunit removes a conserved adenine from the sarcin/ricin loop (SRL), inhibiting protein synthesis. A clear understanding of why Stx2 causes more severe disease compared to Stx1 is lacking. Previous research has focused solely on the role of the B subunit. However, it has been shown that the A1 subunit of Stx2 has higher catalytic activity than A1 subunit of Stx1. Four or five residues involved in electrostatic surface charge differences are interchanged between the A1 subunits of Stx1 and Stx2. It is hypothesized that these residues contribute to the higher activity and toxicity of Stx2A1. The various Shiga toxin constructs under the control of a galactose promoter were transformed into yeast. Stx1 quad and quin show an increase in toxicity at the 1hr time point followed by a decrease at 2hr. This is suggestive of increased toxicity of the Stx1 quad and quin compared to WT Stx1.
NoteM.S.
NoteIncludes bibliographical references
Genretheses
Persistent URLhttps://doi.org/doi:10.7282/t3-j8h6-z233
LanguageEnglish
CollectionSchool of Graduate Studies Electronic Theses and Dissertations
Organization NameRutgers, The State University of New Jersey
RightsThe author owns the copyright to this work.
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