Mutations in the DG loop of adenovirus type 5 fiber knob protein abolish high-affinity binding to its cellular receptor CAR.

@article{Kirby1999MutationsIT,
  title={Mutations in the DG loop of adenovirus type 5 fiber knob protein abolish high-affinity binding to its cellular receptor CAR.},
  author={Ian K. Kirby and Elizabeth Davison and Andrew J Beavil and Cecilia P C Soh and Thomas J. Wickham and Peter W. Roelvink and Imi Kovesdi and Brian J. Sutton and George Santis},
  journal={Journal of virology},
  year={1999},
  volume={73 11},
  pages={9508-14}
}
The amino acid residues in adenovirus type 5 (Ad5) fiber that interact with its cellular receptor, the coxsackie B virus and Ad receptor (CAR), have not been defined. To investigate this, multiple mutations were constructed in the region between residues 479 and 497 in Ad5 fiber (beta-strands E and F and the adjacent region of the DG loop). The effects of these mutations on binding to CAR were determined by use of cell-binding competition experiments, surface plasmon resonance, and direct… CONTINUE READING