8FCG
Cryo-EM structure of Chikungunya virus asymmetric unit
This is a non-PDB format compatible entry.
Summary for 8FCG
| Entry DOI | 10.2210/pdb8fcg/pdb |
| EMDB information | 28979 |
| Descriptor | E1 glycoprotein, E2 glycoprotein, Capsid protein, ... (4 entities in total) |
| Functional Keywords | chikv asymmetric unit, virus |
| Biological source | Chikungunya virus More |
| Total number of polymer chains | 12 |
| Total formula weight | 447952.53 |
| Authors | Su, G.C.,Chmielewsk, D.,Kaelber, J.,Pintilie, G.,Chen, M.,Jin, J.,Auguste, A.,Chiu, W. (deposition date: 2022-12-01, release date: 2024-03-20, Last modification date: 2024-04-03) |
| Primary citation | Chmielewski, D.,Su, G.C.,Kaelber, J.T.,Pintilie, G.D.,Chen, M.,Jin, J.,Auguste, A.J.,Chiu, W. Cryogenic electron microscopy and tomography reveal imperfect icosahedral symmetry in alphaviruses. Pnas Nexus, 3:pgae102-pgae102, 2024 Cited by PubMed Abstract: Alphaviruses are spherical, enveloped RNA viruses with two-layered icosahedral architecture. The structures of many alphaviruses have been studied using cryogenic electron microscopy (cryo-EM) reconstructions, which impose icosahedral symmetry on the viral particles. Using cryogenic electron tomography (cryo-ET), we revealed a polarized symmetry defect in the icosahedral lattice of Chikungunya virus (CHIKV) in situ, similar to the late budding particles, suggesting the inherent imperfect symmetry originates from the final pinch-off of assembled virions. We further demonstrated this imperfect symmetry is also present in in vitro purified CHIKV and Mayaro virus, another arthritogenic alphavirus. We employed a subparticle-based single-particle analysis protocol to circumvent the icosahedral imperfection and boosted the resolution of the structure of the CHIKV to ∼3 Å resolution, which revealed detailed molecular interactions between glycoprotein E1-E2 heterodimers in the transmembrane region and multiple lipid-like pocket factors located in a highly conserved hydrophobic pocket. This complementary use of in situ cryo-ET and single-particle cryo-EM approaches provides a more precise structural description of near-icosahedral viruses and valuable insights to guide the development of structure-based antiviral therapies against alphaviruses. PubMed: 38525304DOI: 10.1093/pnasnexus/pgae102 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.09 Å) |
Structure validation
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