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TitleStructural polymorphism of two-dimensional lattices assembled from baculoviral capsid proteins.
Journal, issue, pagesVirol Sin, Vol. 40, Issue 6, Page 935-945, Year 2025
Publish dateNov 19, 2025
AuthorsKexing Tian / Heya Na / Yan Fu / Tingting Chong / Chao Leng / Fanxing Meng / Yaozhou Liang / Manli Wang / Zhihong Hu / Xi Wang / Guibo Rao / Sheng Cao /
PubMed AbstractProtein nanotubes (PNTs) can be regarded as two-dimensional (2D) lattices with p1 or p2 symmetry rolled into tubes. However, attempts to re-assemble their building blocks into stable 2D nanomaterials ...Protein nanotubes (PNTs) can be regarded as two-dimensional (2D) lattices with p1 or p2 symmetry rolled into tubes. However, attempts to re-assemble their building blocks into stable 2D nanomaterials often fail. Here, starting from two baculoviral capsid proteins, we screened protein variants for the in vitro assembly of various nanotubes and nanosheets. These high-order assemblies were structurally characterized by cryo-electron microscopy techniques. Interfacial analysis of three groups of PNTs revealed that helical heterogeneity is largely the result of the redundancy of p2 symmetry-related contacting interfaces. The assembled nanosheets showed similar interfacial networks to their nanotubular counterparts. In addition, foreign macromolecules could be efficiently displayed on the size-controllable double-layered nanosheets. This study sheds light on the rational design of flexible nanosheets, and it also provides novel 2D protein scaffolds for developing biocompatible materials.
External linksVirol Sin / PubMed:41265796
MethodsEM (helical sym.) / EM (single particle)
Resolution2.8 - 6.6 Å
Structure data

EMDB-39489: Cryo-EM structure of H11 nanotubes assembled from baculovirus capsid protein
Method: EM (helical sym.) / Resolution: 3.2 Å

EMDB-39492: Cryo-EM structure of H12 nanotubes assembled from baculovirus capsid protein
Method: EM (helical sym.) / Resolution: 3.6 Å

EMDB-61711: H14 nanotubes assembled from baculovirus capsid protein
Method: EM (helical sym.) / Resolution: 3.8 Å

61712

9jpr

EMDB-61712, PDB-9jpr:
Local refinement of H11 nanotubes assembled from baculovirus capsid protein
Method: EM (single particle) / Resolution: 2.8 Å

61713

9jps

EMDB-61713, PDB-9jps:
Local refinement of H12 nanotubes assembled from baculovirus capsid protein
Method: EM (single particle) / Resolution: 3.3 Å

61714

9jpt

EMDB-61714, PDB-9jpt:
Local refinement of H14 nanotubes assembled from baculovirus capsid protein
Method: EM (single particle) / Resolution: 3.4 Å

EMDB-61996: A7 nanotubes assembled from baculovirus capsid protein
Method: EM (helical sym.) / Resolution: 6.6 Å

61997

9k2o

EMDB-61997, PDB-9k2o:
Local refinement of A7 nanotubes assembled from baculovirus capsid protein
Method: EM (single particle) / Resolution: 3.4 Å

Source
  • helicoverpa armigera nucleopolyhedrovirus
  • Autographa californica multiple nucleopolyhedrovirus
  • autographa californica nuclear polyhedrosis virus
  • schistosoma japonicum (invertebrata)
KeywordsVIRAL PROTEIN / capsid protein / self-assembly / Baculovirus / nanotube

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