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	Asymmetric structural transitions in the icosahedral organization of Eastern equine encephalitis virus.
Journal, issue, pages	Nat Commun, Year 2026
Publish date	May 15, 2026
Authors	Abhishek Bandyopadhyay / Lauren E Williamson / Cameron D Buchman / Thomas Klose / James E Crowe / Richard J Kuhn /
PubMed Abstract	Delivery of the viral genome into host cells is a critical step in successful viral infection. Alphaviruses achieve this step by fusing the viral and endosomal membranes under acidic conditions. This ...Delivery of the viral genome into host cells is a critical step in successful viral infection. Alphaviruses achieve this step by fusing the viral and endosomal membranes under acidic conditions. This process requires significant structural changes in the alphavirus glycoprotein organization. Structural characterization of acidic pH-induced conformational changes in alphavirus virions has remained elusive due to the rapid, transient nature of these states, conformational heterogeneity, and particle aggregation. Antibody binding studies conducted at elevated temperatures or under acidic pH conditions have further revealed the presence of transitional epitopes that are inaccessible on alphaviruses at room temperature or neutral pH. In this report, we present structural snapshots of the conformational changes in the glycoproteins and nucleocapsid core of a prototypical alphavirus, Eastern equine encephalitis virus, caused by exposure to 40 °C or pH 5.6. These findings provide insights into the structural transitions that occur prior to viral fusion with the endosomal membrane. This approach has also allowed us to define the molecular basis for recognition of a pan-alphavirus epitope by a patient-derived human antibody.
External links	Nat Commun / PubMed:42140932
Methods	EM (single particle)
Resolution	3.1 - 11.3 Å
Structure data	72740 9yaw EMDB-72740, PDB-9yaw: Localized reconstruction of the asymmetric unit of SINV/EEEV in complex with Fab EEEV-33 at arm 4 at pH 5.6. Method: EM (single particle) / Resolution: 4.2 Å 72741 9yax EMDB-72741, PDB-9yax: Localized reconstruction of the asymmetric unit of the low pH treated back neutralized SINV/EEEV in complex with Fab fragment of the antibody EEEV-179 Method: EM (single particle) / Resolution: 4.2 Å 72743 9yaz EMDB-72743, PDB-9yaz: Localized reconstruction of the asymmetric unit of SINV/EEEV in complex with Fab EEEV-179 at 40C sample. Method: EM (single particle) / Resolution: 3.8 Å 72745 9yb1 EMDB-72745, PDB-9yb1: Localized reconstruction of the asymmetric unit of SINV/EEEV at pH 5.6. Method: EM (single particle) / Resolution: 4.7 Å 72746 9yb2 EMDB-72746, PDB-9yb2: Localized reconstruction of the asymmetric unit of SINV/EEEV at 40C sample. Method: EM (single particle) / Resolution: 4.1 Å 72747 9yb3 EMDB-72747, PDB-9yb3: Localized reconstruction of the asymmetric unit of SINV/EEEV. Method: EM (single particle) / Resolution: 3.6 Å 72748 9yb4 EMDB-72748, PDB-9yb4: Localized reconstruction of the asymmetric unit of the low pH treated back neutralized SINV/EEEV. Method: EM (single particle) / Resolution: 3.1 Å EMDB-73016: Icosahedral reconstruction of EEEV at pH 5.6. Method: EM (single particle) / Resolution: 10.4 Å EMDB-73024: EEEV + EEEV-179 Fab at pH 5.6 Method: EM (single particle) / Resolution: 11.3 Å
Chemicals	ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose
Source	homo sapiens (human) eastern equine encephalitis virus
Keywords	VIRUS / Eastern Equine Encephalitis Virus / Cryo-EM / Single Particle Averaging / localized reconstruction / asymmetric unit / low pH back neutralization. / 40C. / asymmetric unit.