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TitleCryo-EM structures of Banna virus in multiple states reveal stepwise detachment of viral spikes.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 2284, Year 2024
Publish dateMar 13, 2024
AuthorsZhiqiang Li / Han Xia / Guibo Rao / Yan Fu / Tingting Chong / Kexing Tian / Zhiming Yuan / Sheng Cao /
PubMed AbstractBanna virus (BAV) is the prototype Seadornavirus, a class of reoviruses for which there has been little structural study. Here, we report atomic cryo-EM structures of three states of BAV virions- ...Banna virus (BAV) is the prototype Seadornavirus, a class of reoviruses for which there has been little structural study. Here, we report atomic cryo-EM structures of three states of BAV virions-surrounded by 120 spikes (full virions), 60 spikes (partial virions), or no spikes (cores). BAV cores are double-layered particles similar to the cores of other non-turreted reoviruses, except for an additional protein component in the outer capsid shell, VP10. VP10 was identified to be a cementing protein that plays a pivotal role in the assembly of BAV virions by directly interacting with VP2 (inner capsid), VP8 (outer capsid), and VP4 (spike). Viral spikes (VP4/VP9 heterohexamers) are situated on top of VP10 molecules in full or partial virions. Asymmetrical electrostatic interactions between VP10 monomers and VP4 trimers are disrupted by high pH treatment, which is thus a simple way to produce BAV cores. Low pH treatment of BAV virions removes only the flexible receptor binding protein VP9 and triggers significant conformational changes in the membrane penetration protein VP4. BAV virions adopt distinct spatial organization of their surface proteins compared with other well-studied reoviruses, suggesting that BAV may have a unique mechanism of penetration of cellular endomembranes.
External linksNat Commun / PubMed:38480794 / PubMed Central
MethodsEM (single particle)
Resolution2.64 - 5.7 Å
Structure data

36870

8k42

EMDB-36870, PDB-8k42:
Structure of full Banna virus
Method: EM (single particle) / Resolution: 2.64 Å

36871

8k43

EMDB-36871, PDB-8k43:
In situ structure of RNA-dependent RNA polymerase in full BAV particles
Method: EM (single particle) / Resolution: 3.0 Å

36872

8k44

EMDB-36872, PDB-8k44:
Structure of VP9 in Banna virus
Method: EM (single particle) / Resolution: 3.8 Å

36880

8k49

EMDB-36880, PDB-8k49:
Structure of partial Banna virus
Method: EM (single particle) / Resolution: 2.9 Å

36881

8k4a

EMDB-36881, PDB-8k4a:
Structure of Banna virus core
Method: EM (single particle) / Resolution: 2.64 Å

37378

8w9p

EMDB-37378, PDB-8w9p:
Structure of full Banna virus
Method: EM (single particle) / Resolution: 2.7 Å

37379

8w9q

EMDB-37379, PDB-8w9q:
Structure of partial Banna virus
Method: EM (single particle) / Resolution: 5.7 Å

37380

8w9r

EMDB-37380, PDB-8w9r:
Structure of Banna virus core
Method: EM (single particle) / Resolution: 4.8 Å

Source
  • banna virus
KeywordsVIRUS / reovirus / complex / capsid protein / RdRp / inner capsid protein / VIRAL PROTEIN / receptor binding / spike / intermediate state / core particle

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