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Structure paper

TitleConformational shift of a major poliovirus antigen confirmed by immuno-cryogenic electron microscopy.
Journal, issue, pagesJ Immunol, Vol. 191, Issue 2, Page 884-891, Year 2013
Publish dateJul 15, 2013
AuthorsJun Lin / Naiqian Cheng / James M Hogle / Alasdair C Steven / David M Belnap /
PubMed AbstractSmall, interfacial conformational changes occur in some Ag-Ab interactions. Using cryogenic electron microscopy (cryo-EM), we have demonstrated such changes in a major antigenic site of a poliovirus ...Small, interfacial conformational changes occur in some Ag-Ab interactions. Using cryogenic electron microscopy (cryo-EM), we have demonstrated such changes in a major antigenic site of a poliovirus capsid protein. During cell entry, native human poliovirus (160S particle) converts to a cell entry intermediate (135S particle) and later to an RNA-released (80S) particle. By mixing particles with Fabs of the neutralizing C3 mAb, we labeled the external loop connecting the B and C β-strands (BC loop) of the capsid protein VP1 (residues 95-105) in the 160S and 135S states. We then determined three-dimensional structures by cryo-EM and enhanced their interpretability by fitting high-resolution coordinates of C3 Fab and the capsid proteins into the density maps. Binding of C3 to either 160S or 135S particles caused residues of the BC loop, located on the tip of a prominent peak known as the "mesa," to move by an estimated 5 Å. C3 Abs are neutralizing and can bind bivalently. The orientation of the bound Fabs in our reconstructions suggests that C3 neutralizes poliovirus by binding two adjacent BC loops on the same mesa and inhibiting conformational changes in the viral capsid.
External linksJ Immunol / PubMed:23772035 / PubMed Central
MethodsEM (single particle)
Resolution9.1 - 22.0 Å
Structure data

5291

3j3o

EMDB-5291: Poliovirus 160S particle and C3 Fab complex at 11.1 Angstrom resolution
PDB-3j3o: Conformational Shift of a Major Poliovirus Antigen Confirmed by Immuno-Cryogenic Electron Microscopy: 160S Poliovirus and C3-Fab Complex
Method: EM (single particle) / Resolution: 11.1 Å

5292

3j3p

EMDB-5292: Poliovirus 135S particle and C3 Fab complex at 9.1 Angstrom resolution
PDB-3j3p: Conformational Shift of a Major Poliovirus Antigen Confirmed by Immuno-Cryogenic Electron Microscopy: 135S Poliovirus and C3-Fab Complex
Method: EM (single particle) / Resolution: 9.1 Å

EMDB-5293:
Poliovirus 80S particle and C3 Fab complex at 22 Angstrom resolution
Method: EM (single particle) / Resolution: 22.0 Å

Chemicals

ChemComp-SPH:
SPHINGOSINE / Sphingosine

ChemComp-MYR:
MYRISTIC ACID / Myristic acid

Source
  • mus musculus (house mouse)
  • unidentified (others)
  • human poliovirus 1
KeywordsVIRUS/IMMUNE SYSTEM / antibody-antigen interaction / antibody-protein interaction / picornavirus / virus-antibody interaction / neutralizing antibody interaction / conformational change / VIRUS-IMMUNE SYSTEM complex / 135S cell-entry intermediate particle / antibody neutralization

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