Toroidal surface complexes of bacteriophage Φ12 are responsible for host-cell attachment

Alejandra Leo-Macias, Garrett Katz, Hui Wei, Alexandra Alimova, A. Katz, William J. Rice, Ruben Diaz-Avalos, Guo Bin Hu, David L. Stokes, Paul Gottlieb

Research output: Contribution to journalArticlepeer-review

14 Scopus citations


Cryo-electron tomography and subtomogram averaging are utilized to determine that the bacteriophage Φ12, a member of the Cystoviridae family, contains surface complexes that are toroidal in shape, are composed of six globular domains with six-fold symmetry, and have a discrete density connecting them to the virus membrane-envelope surface. The lack of this kind of spike in a reassortant of Φ12 demonstrates that the gene for the hexameric spike is located in Φ12's medium length genome segment, likely to the P3 open reading frames which are the proteins involved in viral-host cell attachment. Based on this and on protein mass estimates derived from the obtained averaged structure, it is suggested that each of the globular domains is most likely composed of a total of four copies of P3a and/or P3c proteins. Our findings may have implications in the study of the evolution of the cystovirus species in regard to their host specificity.

Original languageEnglish (US)
Pages (from-to)103-109
Number of pages7
Issue number2
StatePublished - Jun 5 2011
Externally publishedYes


  • Cryo-electron tomography
  • Cystovirus
  • Subtomogram averaging
  • Φ12 six-fold symmetry
  • Φ12 surface proteins

ASJC Scopus subject areas

  • Virology


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