- Library Home /
- Search Collections /
- Open Collections /
- Browse Collections /
- UBC Theses and Dissertations /
- The role of toxic shock syndrome Toxin-1 and Staphylococcal...
Open Collections
UBC Theses and Dissertations
UBC Theses and Dissertations
The role of toxic shock syndrome Toxin-1 and Staphylococcal Enterotoxin A in the pathogenesis of toxic shock syndrome Chang, Alex Hongsheng
Abstract
Toxic shock syndrome (TSS) is a multisystem disease associated with S. aureus infection. Toxic shock syndrometoxin-1 (TSST-1) is implicated in the majority but not all cases. We have previously demonstrated that sero \conversion to staphylococcal enterotoxin A (SEA) is also more prevalent in TSS than in non-TSS cases, suggesting its possible role in TSS. Previous studies have demonstrated that TSST-1 and SEA are super antigens, which bind directly to class II molecules on antigen presenting cells, and stimulates T cells bearing specific VB sequences. Whether there are direct binding sites for TSST-1 and SEA on human resting T cells remains unclear. Three approaches were taken to further examine the role of TSST-1 and SEA in the pathogenesis of TSS: a) to detect TSST-1 and staphylococcal enterotoxin A (SEA) in the culture supernatants of S. aureus by ELISA method, in order to study the production of TSST-1and SEA among 350 isolates of S. aureus collected from TSS patients and other individuals; b) to characterize the distribution of these isolates by multilocus enzyme electrophoresis at 19 enzyme chromosomal loci; and c) to characterize receptor-mediated binding of TSST-1 and SEA to human T cells, to confirm whether there are direct TSST-1and SEA binding sites on resting T lymphocytes, to study the [More abstract follows]
Item Metadata
Title |
The role of toxic shock syndrome Toxin-1 and Staphylococcal Enterotoxin A in the pathogenesis of toxic shock syndrome
|
Creator | |
Publisher |
University of British Columbia
|
Date Issued |
1992
|
Description |
Toxic shock syndrome (TSS) is a multisystem disease associated with S. aureus infection. Toxic shock syndrometoxin-1 (TSST-1) is implicated in the majority but not all cases. We have previously demonstrated that sero \conversion to staphylococcal enterotoxin A (SEA) is also more prevalent in TSS than in non-TSS cases, suggesting its possible role in TSS. Previous studies have demonstrated that TSST-1 and SEA are super antigens, which bind directly to class II molecules on antigen presenting cells, and stimulates T cells bearing specific VB sequences. Whether there are direct binding sites for TSST-1 and SEA on human resting T cells remains unclear. Three approaches were taken to further examine the role of TSST-1 and SEA in the pathogenesis of TSS: a) to detect TSST-1 and staphylococcal enterotoxin A (SEA) in the culture supernatants of S. aureus by ELISA method, in order to study the production of TSST-1and SEA among 350 isolates of S. aureus collected from TSS patients and other individuals; b) to characterize the distribution of these isolates by multilocus enzyme electrophoresis at 19 enzyme chromosomal loci; and c) to characterize receptor-mediated binding of TSST-1 and SEA to human T cells, to confirm whether there are direct TSST-1and SEA binding sites on resting T lymphocytes, to study the
[More abstract follows]
|
Extent |
4962738 bytes
|
Genre | |
Type | |
File Format |
application/pdf
|
Language |
eng
|
Date Available |
2008-12-23
|
Provider |
Vancouver : University of British Columbia Library
|
Rights |
For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use.
|
DOI |
10.14288/1.0098902
|
URI | |
Degree | |
Program | |
Affiliation | |
Degree Grantor |
University of British Columbia
|
Graduation Date |
1992-05
|
Campus | |
Scholarly Level |
Graduate
|
Aggregated Source Repository |
DSpace
|
Item Media
Item Citations and Data
Rights
For non-commercial purposes only, such as research, private study and education. Additional conditions apply, see Terms of Use https://open.library.ubc.ca/terms_of_use.