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

spinqualitylabelsall models 9yax, resolution 4.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9yax is a 17 chain structure with sequence from Eastern equine encephalitis virus and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 4.2Å Ligands: BMA, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function W8RHT7_EEEV Provides the signal sequence for the translocation of the precursor of protein E3/E2 to the host endoplasmic reticulum. Furin-cleaved E3 remains associated with spike glycoprotein E1 and mediates pH protection of the latter during the transport via the secretory pathway. After virion release from the host cell, the assembly protein E3 is gradually released in the extracellular space.[ARBA:ARBA00037518] Publication Abstract from PubMed 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 degrees 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. Asymmetric structural transitions in the icosahedral organization of Eastern equine encephalitis virus.,Bandyopadhyay A, Williamson LE, Buchman CD, Klose T, Crowe JE Jr, Kuhn RJ Nat Commun. 2026 May 15. doi: 10.1038/s41467-026-73197-8. PMID:42140932 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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