Journal article
Structures of Five Mutants of Toxic Shock Syndrome Toxin-1 with Reduced Biological Activity
Biochemistry (Easton), Vol.37(20), pp.7194-7202
05/19/1998
DOI: 10.1021/bi9721896
PMID: 9585531
Abstract
The three-dimensional structures of five mutants of toxic shock syndrome toxin-1 (TSST-1) have been determined. These mutations are in the long central α helix and are useful in mapping portions of TSST-1 involved in superantigenicity and lethality. The T128A, H135A, Q139K, and I140T mutations appear to reduce superantigenicity by altering the properties of the T-cell receptor interaction surface. The Q136A mutation is at a largely buried site and causes a dramatic change in the conformation of the β7−β9 loop which covers the back of the central α helix. As this mutation has the unique ability to reduce the toxin's lethality in rabbits while retaining its superantigenicity, it raises the possibility that this rear loop mediates the ability of TSST-1 to induce lethality and suggests a route for producing nonlethal toxins for therapeutic development.
Details
- Title: Subtitle
- Structures of Five Mutants of Toxic Shock Syndrome Toxin-1 with Reduced Biological Activity
- Creators
- Cathleen A EarhartDavid T MitchellDebra L MurrayDenise M PinheiroMasazumi MatsumuraPatrick M SchlievertDouglas H Ohlendorf
- Resource Type
- Journal article
- Publication Details
- Biochemistry (Easton), Vol.37(20), pp.7194-7202
- Publisher
- American Chemical Society
- DOI
- 10.1021/bi9721896
- PMID
- 9585531
- ISSN
- 0006-2960
- eISSN
- 1520-4995
- Language
- English
- Date published
- 05/19/1998
- Academic Unit
- Microbiology and Immunology; Internal Medicine
- Record Identifier
- 9984001139902771
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