The Hypervariable D3 Domain of Salmonella Flagellin Is an Autonomous Folding Unit

Title: The Hypervariable D3 Domain of Salmonella Flagellin Is an Autonomous Folding Unit

Volume: 15 Issue: 1

Author(s): Ferenc Vonderviszt, Anett Sebestyen, Adel Muskotal and Barbara M. Vegh

Affiliation:

Keywords: Flagellin, D3 domain, scanning calorimetry, protein scaffold

Abstract: The hypervariable D3 domain of Salmonella flagellin, composed of the 190-285 segment, is the major determinant of flagellar antigenicity. D3 was cloned and overexpressed in E. coli. Although previous studies concluded that D3 is stabilized by interactions with the D2 domain, our calorimetric experiments have revealed that isolated D3 has a stable tertiary structure which is highly resistant against proteolytic digestion. Repeated heating experiments demonstrated that unfolding of D3 is reversible. Its small size and stable structure makes D3 a promising protein scaffold for the development of artificial binding proteins by directed evolution.

Cite this article as:

Vonderviszt Ferenc, Sebestyen Anett, Muskotal Adel and Vegh M. Barbara, The Hypervariable D3 Domain of Salmonella Flagellin Is an Autonomous Folding Unit, Protein & Peptide Letters 2008; 15 (1) . https://dx.doi.org/10.2174/092986608783330440

DOI https://dx.doi.org/10.2174/092986608783330440	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305