Three-dimensional reconstructions of the bacteriophage CUS-3 virion reveal a conserved coat protein I-domain but a distinct tailspike receptor-binding domain.

Kristin N Parent, Jinghua Tang, Giovanni Cardone, Eddie B Gilcrease, Mandy E Janssen, Norman H Olson, Sherwood R Casjens, Timothy S Baker

Virology 2014 Sep

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CUS-3 is a short-tailed, dsDNA bacteriophage that infects serotype K1 Escherichia coli. We report icosahedrally averaged and asymmetric, three-dimensional, cryo-electron microscopic reconstructions of the CUS-3 virion. Its coat protein structure adopts the "HK97-fold" shared by other tailed phages and is quite similar to that in phages P22 and Sf6 despite only weak amino acid sequence similarity. In addition, these coat proteins share a unique extra external domain ("I-domain"), suggesting that the group of P22-like phages has evolved over a very long time period without acquiring a new coat protein gene from another phage group. On the other hand, the morphology of the CUS-3 tailspike differs significantly from that of P22 or Sf6, but is similar to the tailspike of phage K1F, a member of the extremely distantly related T7 group of phages. We conclude that CUS-3 obtained its tailspike gene from a distantly related phage quite recently. Copyright © 2014 Elsevier Inc. All rights reserved.

Citation

Kristin N Parent, Jinghua Tang, Giovanni Cardone, Eddie B Gilcrease, Mandy E Janssen, Norman H Olson, Sherwood R Casjens, Timothy S Baker. Three-dimensional reconstructions of the bacteriophage CUS-3 virion reveal a conserved coat protein I-domain but a distinct tailspike receptor-binding domain. Virology. 2014 Sep;464-465:55-66