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TitleA stargate mechanism of genome delivery unveiled by cryogenic electron tomography.
Journal, issue, pagesbioRxiv, Year 2024
Publish dateJun 11, 2024
AuthorsPavol Bardy / Conor I W MacDonald / Paul C Kirchberger / Huw T Jenkins / Tibor Botka / Lewis Byrom / Nawshin T B Alim / Daouda A K Traore / Hannah C König / Tristan R Nicholas / Maria Chechik / Samuel J Hart / Johan P Turkenburg / James N Blaza / J Thomas Beatty / Paul C M Fogg / Alfred A Antson /
PubMed AbstractSingle-stranded DNA bacteriophages of the family are major components of the global virosphere. Microviruses are highly abundant in aquatic ecosystems and are prominent members of the mammalian gut ...Single-stranded DNA bacteriophages of the family are major components of the global virosphere. Microviruses are highly abundant in aquatic ecosystems and are prominent members of the mammalian gut microbiome, where their diversity has been linked to various chronic health disorders. Despite the clear importance of microviruses, little is known about the molecular mechanism of host infection. Here, we have characterized an exceptionally large microvirus, Ebor, and provide crucial insights into long-standing mechanistic questions. Cryogenic electron microscopy of Ebor revealed a capsid with trimeric protrusions that recognise lipopolysaccharides on the host surface. Cryogenic electron tomography of the host cell colonized with virus particles demonstrated that the virus initially attaches to the cell via five such protrusions, located at the corners of a single pentamer. This interaction triggers a stargate mechanism of capsid opening along the 5-fold symmetry axis, enabling delivery of the virus genome. Despite variations in specific virus-host interactions among different family viruses, structural data indicate that the stargate mechanism of infection is universally employed by all members of the family. Startlingly, our data reveal a mechanistic link for the opening of relatively small capsids made out of a single jelly-roll fold with the structurally unrelated giant viruses.
External linksbioRxiv / PubMed:38915634 / PubMed Central
MethodsEM (single particle) / EM (subtomogram averaging)
Resolution3.2 - 31.0 Å
Structure data

50356

9ffg

EMDB-50356, PDB-9ffg:
Empty capsid of Rhodobacter microvirus Ebor computed with I4 symmetry
Method: EM (single particle) / Resolution: 3.3 Å

50357

9ffh

EMDB-50357, PDB-9ffh:
Native capsid of Rhodobacter microvirus Ebor computed with I4 symmetry
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-50358: In vitro-induced genome-releasing intermediate of Rhodobacter microvirus Ebor computed with C5 symmetry
Method: EM (single particle) / Resolution: 25.0 Å

EMDB-50359: Rhodobacter microvirus Ebor attached to B10 host cell reconstructed by single particle analysis with applied C5 symmetry
Method: EM (single particle) / Resolution: 7.84 Å

EMDB-50360: Rhodobacter microvirus Ebor attached to the outer membrane vesicle
Method: EM (subtomogram averaging) / Resolution: 13.2 Å

EMDB-50361: Rhodobacter microvirus Ebor attached to the host cell reconstructed by subtomogram averaging
Method: EM (subtomogram averaging) / Resolution: 31.0 Å

Source
  • rhodobacter capsulatus (bacteria)
  • rhodobacter capsulatus sb 1003 (bacteria)
KeywordsVIRUS / ssDNA virus / Microviridae / Tainavirinae / Alphaproteobacteria / Rhodobacter capsulatus / aquatic virus / jelly-roll fold

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