8Y3T

The self-assembled nanotube of CPC46A/Q70H

Summary for 8Y3T

• Entry DOI: 10.2210/pdb8y3t/pdb
• Related: 8Y3N
• EMDB information: 38898
• Descriptor: Capsid protein (1 entity in total)
• Functional Keywords: capsid protein, self-assembly, nanotube, viral protein
• Biological source: Emesvirus zinderi
• Total number of polymer chains: 2
• Total formula weight: 27432.83

Authors

Yang, M.,Rao, G.,Li, L.,Qi, L.,Ma, C.,Zhang, H.,Gong, J.,Wei, B.,Zhang, X.E.,Chen, G.,Cao, S.,Li, F. (deposition date: 2024-01-29, release date: 2024-11-06)

Primary citation

Yang, M.,Rao, G.,Li, L.,Qi, L.,Ma, C.,Zhang, H.,Gong, J.,Wei, B.,Zhang, X.E.,Chen, G.,Cao, S.,Li, F.
Transformation of a Viral Capsid from Nanocages to Nanotubes and Then to Hydrogels: Redirected Self-Assembly and Effects on Immunogenicity.
Acs Nano, 18:13755-13767, 2024

PubMed Abstract: The ability to manipulate the self-assembly of proteins is essential to understanding the mechanisms of life and beneficial to fabricating advanced nanomaterials. Here, we report the transformation of the MS2 phage capsid from nanocages to nanotubes and then to nanotube hydrogels through simple point mutations guided by interfacial interaction redesign. We demonstrate that site 70, which lies in the flexible FG loop of the capsid protein (CP), is a "magic" site that can largely dictate the final morphology of assemblies. By varying the amino acid at site 70, with the aid of a cysteine-to-alanine mutation at site 46, we achieved the assembly of double-helical or single-helical nanotubes in addition to nanocages. Furthermore, an additional cysteine substitution on the surface of nanotubes mediated their cross-linking to form hydrogels with reducing agent responsiveness. The hierarchical self-assembly system allowed for the investigation of morphology-related immunogenicity of MS2 CPs, which revealed dramatic differences among nanocages, nanotubes, and nanotube hydrogels in terms of immune response types, antibody levels and T cell functions. This study provides insights into the assembly manipulation of protein nanomaterials and the customized design of nanovaccines and drug delivery systems.

PubMed: 38752610
DOI: 10.1021/acsnano.4c01969

Experimental method

ELECTRON MICROSCOPY (2.61 Å)