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

Zhang P, Mueller S, Morais MC, Bator CM, Bowman VD, Hafenstein S, Wimmer E, Rossmann MG
Proc Natl Acad Sci U S A 105 18284-9 (2008)
Related entries: 3epc, 3epd, 3uro

Cited: 60 times
EuropePMC logo PMID: 19011098

Abstract

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-A resolution and fitted into approximately 8.5-A 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.

Articles - 3epf mentioned but not cited (3)

  1. Identification of site-specific adaptations conferring increased neural cell tropism during human enterovirus 71 infection. Cordey S, Petty TJ, Schibler M, Martinez Y, Gerlach D, van Belle S, Turin L, Zdobnov E, Kaiser L, Tapparel C. PLoS Pathog 8 e1002826 (2012)
  2. Crystal structure of CD155 and electron microscopic studies of its complexes with polioviruses. Zhang P, Mueller S, Morais MC, Bator CM, Bowman VD, Hafenstein S, Wimmer E, Rossmann MG. Proc Natl Acad Sci U S A 105 18284-18289 (2008)
  3. Kinetic and structural analysis of coxsackievirus B3 receptor interactions and formation of the A-particle. Organtini LJ, Makhov AM, Conway JF, Hafenstein S, Carson SD. J Virol 88 5755-5765 (2014)


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