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Salmonella Phage S16 Tail Fiber Adhesin Features a Rare Polyglycine Rich Domain for Host Recognition.

  • Dunne M Institute of Food, Nutrition and Health, ETH Zurich, Zurich, Switzerland. Electronic address: matthew.dunne@hest.ethz.ch.
  • Denyes JM Institute of Food, Nutrition and Health, ETH Zurich, Zurich, Switzerland.
  • Arndt H Institute of Food, Nutrition and Health, ETH Zurich, Zurich, Switzerland.
  • Loessner MJ Institute of Food, Nutrition and Health, ETH Zurich, Zurich, Switzerland.
  • Leiman PG Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, 301 University Boulevard, Galveston, TX, USA.
  • Klumpp J Institute of Food, Nutrition and Health, ETH Zurich, Zurich, Switzerland.
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  • 2018-09-25
Published in:
  • Structure (London, England : 1993). - 2018
Salmonella
X-ray crystallography
bacteriophage
polyglycine sandwich
polyglycine type II helix
Binding Sites
Computer Simulation
Crystallography, X-Ray
Hydrophobic and Hydrophilic Interactions
Models, Molecular
Peptides
Protein Conformation
Protein Domains
Salmonella Phages
Viral Tail Proteins
English The ability of phages to infect specific bacteria has led to their exploitation as bio-tools for bacterial remediation and detection. Many phages recognize bacterial hosts via adhesin tips of their long tail fibers (LTFs). Adhesin sequence plasticity modulates receptor specificity, and thus primarily defines a phage's host range. Here we present the crystal structure of an adhesin (gp38) attached to a trimeric β-helical tip (gp37) from the Salmonella phage S16 LTF. Gp38 contains rare polyglycine type II helices folded into a packed lattice, herein designated "PGII sandwich." Sequence variability within the domain is limited to surface-exposed helices and distal loops that form putative receptor-binding sites. In silico analyses revealed a prevalence of the adhesin architecture among T-even phages, excluding the archetypal T4 phage. Overall, S16 LTF provides a valuable model for understanding binding mechanisms of phage adhesins, and for engineering of phage adhesins with expandable or modulated host ranges.
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  • English
Open access status
bronze
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Persistent URL
https://sonar.ch/global/documents/57856
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