Prokaryotic homologs of the major vault protein form engineerable vault nanocapsules

Prokaryotic and bacteriophage MVP homologs assemble into vault particles, with the phage homolog L05 forming a 96-chain shell enclosing a volume ~25% larger than human vaults.

• Why it matters: Vault function is still unclear, and it was unknown whether prokaryotic MVP homologs can build vault-like particles.
• What they did: The authors surveyed ~15 billion proteins to find MVP homologs across 29 bacterial and 4 archaeal phyla, then used size-exclusion chromatography to screen eight homologs expressed in Escherichia coli.
• The result: Cryo-EM structures of L05 show a defined shell architecture, and altering wall repeats increases vault size, enabling a size-tunable scaffold for cargo encapsulation and vault-assembly studies.

AI summary of the abstract · may contain errors · not medical advice · read the paper.