Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Cryo-electron Microscopy Structure of the Native Prototype Foamy Virus Glycoprotein and Virus Architecture.
Journal, issue, pages	PLoS Pathog, Vol. 12, Issue 7, Page e1005721, Year 2016
Publish date	Jul 11, 2016
Authors	Grégory Effantin / Leandro F Estrozi / Nick Aschman / Patricia Renesto / Nicole Stanke / Dirk Lindemann / Guy Schoehn / Winfried Weissenhorn /
PubMed Abstract	Foamy viruses (FV) belong to the genus Spumavirus, which forms a distinct lineage in the Retroviridae family. Although the infection in natural hosts and zoonotic transmission to humans is ...Foamy viruses (FV) belong to the genus Spumavirus, which forms a distinct lineage in the Retroviridae family. Although the infection in natural hosts and zoonotic transmission to humans is asymptomatic, FVs can replicate well in human cells making it an attractive gene therapy vector candidate. Here we present cryo-electron microscopy and (cryo-)electron tomography ultrastructural data on purified prototype FV (PFV) and PFV infected cells. Mature PFV particles have a distinct morphology with a capsid of constant dimension as well as a less ordered shell of density between the capsid and the membrane likely formed by the Gag N-terminal domain and the cytoplasmic part of the Env leader peptide gp18LP. The viral membrane contains trimeric Env glycoproteins partly arranged in interlocked hexagonal assemblies. In situ 3D reconstruction by subtomogram averaging of wild type Env and of a Env gp48TM- gp80SU cleavage site mutant showed a similar spike architecture as well as stabilization of the hexagonal lattice by clear connections between lower densities of neighboring trimers. Cryo-EM was employed to obtain a 9 Å resolution map of the glycoprotein in its pre-fusion state, which revealed extensive trimer interactions by the receptor binding subunit gp80SU at the top of the spike and three central helices derived from the fusion protein subunit gp48TM. The lower part of Env, presumably composed of interlaced parts of gp48TM, gp80SU and gp18LP anchors the spike at the membrane. We propose that the gp48TM density continues into three central transmembrane helices, which interact with three outer transmembrane helices derived from gp18LP. Our ultrastructural data and 9 Å resolution glycoprotein structure provide important new insights into the molecular architecture of PFV and its distinct evolutionary relationship with other members of the Retroviridae.
External links	PLoS Pathog / PubMed:27399201 / PubMed Central
Methods	EM (subtomogram averaging) / EM (single particle)
Resolution	8.8 - 32.0 Å
Structure data	EMDB-4006: Structure of wt PFV glycoprotein by cryo-electron tomography Method: EM (subtomogram averaging) / Resolution: 32.0 Å EMDB-4007: Structure of iFuse PFV glycoprotein by cryo-electron tomography Method: EM (subtomogram averaging) / Resolution: 28.0 Å EMDB-4008: Structure of the wt PFV glycoprotein from the iNAB Gag mutant by cryo-electron tomography Method: EM (subtomogram averaging) / Resolution: 29.0 Å EMDB-4010: Structure of a hexagonal assembly of the wt PFV glycoprotein from the iNAB Gag mutant by cryo-electron microscopy Method: EM (single particle) / Resolution: 11.7 Å EMDB-4011: Structure of a hexagonal assembly of the wt PFV glycoprotein from the iNAB Gag mutant by cryo-electron microscopy Method: EM (single particle) / Resolution: 9.1 Å EMDB-4012: Structure of a hexagonal assembly of the PFV glycoprotein from the iFuse Env mutant by cryo-electron microscopy Method: EM (single particle) / Resolution: 9.8 Å EMDB-4013: Structure of a hexagonal assembly of the PFV glycoprotein from the iFuse Env mutant by cryo-electron microscopy Method: EM (single particle) / Resolution: 8.8 Å