Phage tailspike proteins with beta-solenoid fold as thermostable carbohydrate binding materials
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Updated: Jun 26, 2026

Engineering Antiviral Agents via Surface Plasmon Resonance
Published on: June 14, 2022
Stefanie Barbirz1, Marion Becker, Alexander Freiberg
1Physikalische Biochemie, Universität Potsdam, Karl-Liebknecht-Str. 24-25, 14476 Golm, Germany.
Abstract:
We have investigated the stability of three tailspike proteins (TSPs) from bacteriophages Sf6, P22, and HK620. Tailspikes are rod-like homotrimers with comparable beta-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.
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