Crystal structure of CD155 and electron microscopic studies of its complexes with polioviruses

Ping Zhang, Steffen Mueller, Marc C. Morais, Carol M. Bator, Valorie D. Bowman, Susan Hafenstein, Eckard Wimmer, Michael G. Rossmann

Research output: Contribution to journalArticlepeer-review

69 Scopus citations


When poliovirus (PV) recognizes its receptor, CD155, the virus changes from a 160S to a 135S particle before releasing its genome into the cytoplasm. CD155 is a transmembrane protein with 3 Ig-like extracellular domains, D1-D3, where D1 is recognized by the virus. The crystal structure of D1D2 has been determined to 3.5-Å resolution and fitted into ≈8.5-Å resolution cryoelectron microscopy reconstructions of the virus-receptor complexes for the 3 PV serotypes. These structures show that, compared with human rhinoviruses, the virus-receptor interactions for PVs have a greater dependence on hydrophobic interactions, as might be required for a virus that can inhabit environments of different pH. The pocket factor was shown to remain in the virus during the first recognition stage. The present structures, when combined with earlier mutational investigations, show that in the subsequent entry stage the receptor moves further into the canyon when at a physiological temperature, thereby expelling the pocket factor and separating the viral subunits to form 135S particles. These results provide a detailed analysis of how a nonenveloped virus can enter its host cell.

Original languageEnglish (US)
Pages (from-to)18284-18289
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number47
StatePublished - Nov 25 2008

All Science Journal Classification (ASJC) codes

  • General


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