Phage tailspike proteins with β-solenoid fold as thermostable carbohydrate binding materials

Stefanie Barbirz, Marion Becker, Alexander Freiberg, Robert Seckler

Research output: Contribution to journalArticle

10 Scopus citations

Abstract

We have investigated the stability of three tailspike proteins (TSPs) from bacteriophages Sf6, P22, and HK620. Tailspikes are rod-like homotrimers with comparable β-solenoid folds and similarly high kinetic stability in spite of different amino acid sequences. As tailspikes bind polysaccharides to recognize the bacterial host cell, their stability is required for maintenance of bacteriophage infectivity under harsh extracellular conditions. They resist denaturation by SDS at ambient temperature and their unfolding is slow even in 6 M guanidinium hydrochloride (GdmHCl). This makes them interesting candidates for very stable carbohydrate binding protein materials. A figure is presented.

Original languageEnglish (US)
Pages (from-to)169-173
Number of pages5
JournalMacromolecular Bioscience
Volume9
Issue number2
DOIs
StatePublished - Feb 11 2009

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Keywords

  • Biofibers
  • Carbohydrate binding
  • Protein kinetic stability
  • Tailspike
  • Thermal properties

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry

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