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	Immunogenicity and structures of a rationally designed prefusion MERS-CoV spike antigen.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 114, Issue 35, Page E7348-E7357, Year 2017
Publish date	Aug 29, 2017
Authors	Jesper Pallesen / Nianshuang Wang / Kizzmekia S Corbett / Daniel Wrapp / Robert N Kirchdoerfer / Hannah L Turner / Christopher A Cottrell / Michelle M Becker / Lingshu Wang / Wei Shi / Wing-Pui Kong / Erica L Andres / Arminja N Kettenbach / Mark R Denison / James D Chappell / Barney S Graham / Andrew B Ward / Jason S McLellan /
PubMed Abstract	Middle East respiratory syndrome coronavirus (MERS-CoV) is a lineage C betacoronavirus that since its emergence in 2012 has caused outbreaks in human populations with case-fatality rates of ∼36%. ...Middle East respiratory syndrome coronavirus (MERS-CoV) is a lineage C betacoronavirus that since its emergence in 2012 has caused outbreaks in human populations with case-fatality rates of ∼36%. As in other coronaviruses, the spike (S) glycoprotein of MERS-CoV mediates receptor recognition and membrane fusion and is the primary target of the humoral immune response during infection. Here we use structure-based design to develop a generalizable strategy for retaining coronavirus S proteins in the antigenically optimal prefusion conformation and demonstrate that our engineered immunogen is able to elicit high neutralizing antibody titers against MERS-CoV. We also determined high-resolution structures of the trimeric MERS-CoV S ectodomain in complex with G4, a stem-directed neutralizing antibody. The structures reveal that G4 recognizes a glycosylated loop that is variable among coronaviruses and they define four conformational states of the trimer wherein each receptor-binding domain is either tightly packed at the membrane-distal apex or rotated into a receptor-accessible conformation. Our studies suggest a potential mechanism for fusion initiation through sequential receptor-binding events and provide a foundation for the structure-based design of coronavirus vaccines.
External links	Proc Natl Acad Sci U S A / PubMed:28807998 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	1.57 - 11.5 Å
Structure data	8783 5w9h EMDB-8783: MERS S ectodomain trimer in complex with Fab of neutralizing antibody G4 PDB-5w9h: MERS S ectodomain trimer in complex with variable domain of neutralizing antibody G4 Method: EM (single particle) / Resolution: 4.0 Å 8784 5w9i EMDB-8784: MERS S ectodomain trimer in complex with Fab of neutralizing antibody G4 PDB-5w9i: MERS S ectodomain trimer in complex with variable domain of neutralizing antibody G4 Method: EM (single particle) / Resolution: 3.6 Å 8785 5w9j EMDB-8785: MERS S ectodomain trimer in complex with Fab of neutralizing antibody G4 PDB-5w9j: MERS S ectodomain trimer in complex with variable domain of neutralizing antibody G4 Method: EM (single particle) / Resolution: 4.8 Å 8786 5w9k EMDB-8786: MERS S ectodomain trimer in complex with Fab of neutralizing antibody G4 PDB-5w9k: MERS S ectodomain trimer in complex with variable domain of neutralizing antibody G4 Method: EM (single particle) / Resolution: 4.6 Å 8787 5w9l EMDB-8787: MERS S ectodomain trimer in complex with Fab of neutralizing antibody G4 PDB-5w9l: MERS S ectodomain trimer in complex with variable domain of neutralizing antibody G4 Method: EM (single particle) / Resolution: 4.8 Å 8788 5w9m EMDB-8788: MERS S ectodomain trimer in complex with Fab of neutralizing antibody G4 PDB-5w9m: MERS S ectodomain trimer in complex with variable domain of neutralizing antibody G4 Method: EM (single particle) / Resolution: 4.7 Å 8789 5w9n EMDB-8789: MERS S ectodomain trimer in complex with Fab of neutralizing antibody G4 PDB-5w9n: MERS S ectodomain trimer in complex with variable domain of neutralizing antibody G4 Method: EM (single particle) / Resolution: 5.0 Å 8790 5w9o EMDB-8790: MERS S ectodomain trimer in complex with Fab of neutralizing antibody G4 PDB-5w9o: MERS S ectodomain trimer in complex with variable domain of neutralizing antibody G4 Method: EM (single particle) / Resolution: 4.5 Å 8791 5w9p EMDB-8791: MERS S ectodomain trimer in complex with Fab of neutralizing antibody G4 PDB-5w9p: MERS S ectodomain trimer in complex with variable domain of neutralizing antibody G4 Method: EM (single particle) / Resolution: 4.0 Å EMDB-8792: MERS S ectodomain trimer in complex with Fab of neutralizing antibody G4 Method: EM (single particle) / Resolution: 4.0 Å EMDB-8793: MERS S ectodomain trimer in complex with Fab of neutralizing antibody G4 Method: EM (single particle) / Resolution: 11.5 Å PDB-5vyh: Crystal Structure of MERS-CoV S1 N-terminal Domain Method: X-RAY DIFFRACTION / Resolution: 2 Å PDB-5vzr: Crystal Structure of MERS-CoV neutralizing antibody G4 Fab Method: X-RAY DIFFRACTION / Resolution: 1.57 Å
Chemicals	ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose ChemComp-FOL: FOLIC ACID ChemComp-MPD: (4S)-2-METHYL-2,4-PENTANEDIOL / precipitantYM ChemComp-IMD: IMIDAZOLE ChemComp-HOH: WATER ChemComp-GOL*: GLYCEROL
Source	middle east respiratory syndrome-related coronavirus mus musculus (house mouse) Middle East respiratory syndrome coronavirus
Keywords	VIRAL PROTEIN / fusion glycoprotein / virus / IMMUNE SYSTEM / antibody / neutralizing / Immunogen / peplomer / viral spike / MERS / MERS S protein / G4