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TitleCrystal structure of CD155 and electron microscopic studies of its complexes with polioviruses.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 105, Issue 47, Page 18284-18289, Year 2008
Publish dateNov 25, 2008
AuthorsPing Zhang / Steffen Mueller / Marc C Morais / Carol M Bator / Valorie D Bowman / Susan Hafenstein / Eckard Wimmer / Michael G Rossmann /
PubMed AbstractWhen 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 ...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.
External linksProc Natl Acad Sci U S A / PubMed:19011098 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution3.5005 - 9.0 Å
Structure data

EMDB-1562: CryoEM reconstructions of PV3 complexed with deglycosylated CD155
PDB-3epd: CryoEM structure of poliovirus receptor bound to poliovirus type 3
Method: EM (single particle) / Resolution: 9.0 Å

EMDB-1563: CryoEM reconstructions of PV2 complexed with deglycosylated CD155
PDB-3epf: CryoEM structure of poliovirus receptor bound to poliovirus type 2
Method: EM (single particle) / Resolution: 9.0 Å

EMDB-1570: CryoEM reconstructions of PV1 complexed with deglycosylated CD155
PDB-3epc: CryoEM structure of poliovirus receptor bound to poliovirus type 1
Method: EM (single particle) / Resolution: 8.0 Å

PDB-3uro:
Poliovirus receptor CD155 D1D2
Method: X-RAY DIFFRACTION / Resolution: 3.5005 Å

Chemicals

ChemComp-SPH:
SPHINGOSINE

ChemComp-MYR:
MYRISTIC ACID

ChemComp-SC4:
1[2-CHLORO-4-METHOXY-PHENYL-OXYMETHYL]-4-[2,6-DICHLORO-PHENYL-OXYMETHYL]-BENZENE

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • human poliovirus 1 mahoney
  • human poliovirus 3
  • poliovirus type 2
KeywordsVIRUS / CD155 structure Immunoglobulin Superfamily / poliovirus capsid jelly role / Cell adhesion / Cell membrane / Glycoprotein / Host-virus interaction / Immunoglobulin domain / Membrane / Receptor / Secreted / Transmembrane / VIRAL PROTEIN / poliovirus receptor ectodomain / Immunoglobulin Super Family

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