8G1R

A Vibrio cholerae viral satellite enables efficient horizontal transfer by using an external scaffold to assemble hijacked coat proteins into small capsids

Summary for 8G1R

• Entry DOI: 10.2210/pdb8g1r/pdb
• EMDB information: 29675
• Descriptor: major head protein, Serine protease (2 entities in total)
• Functional Keywords: ple, procapsid, virus like particle
• Biological source: Vibrio phage ICP1_2011_A; More
• Total number of polymer chains: 5
• Total formula weight: 186943.24

Authors

Subramanian, S.,Boyd, C.M.,Seed, K.D.,Parent, K.N. (deposition date: 2023-02-02, release date: 2024-01-17, Last modification date: 2024-10-16)

Primary citation

Boyd, C.M.,Subramanian, S.,Dunham, D.T.,Parent, K.N.,Seed, K.D.
A Vibrio cholerae viral satellite maximizes its spread and inhibits phage by remodeling hijacked phage coat proteins into small capsids.
Biorxiv, 2023

PubMed Abstract: Phage satellites commonly remodel capsids they hijack from the phages they parasitize, but only a few mechanisms regulating the change in capsid size have been reported. Here, we investigated how a satellite from , PLE, remodels the capsid it has been predicted to steal from the phage ICP1 (1). We identified that a PLE-encoded protein, TcaP, is both necessary and sufficient to form small capsids during ICP1 infection. Interestingly, we found that PLE is dependent on small capsids for efficient transduction of its genome, making it the first satellite to have this requirement. ICP1 isolates that escaped TcaP-mediated remodeling acquired substitutions in the coat protein, suggesting an interaction between these two proteins. With a procapsid-like-particle (PLP) assembly platform in , we demonstrated that TcaP is a scaffold that regulates the assembly of small capsids. Further, we studied the structure of PLE PLPs using cryogenic electron microscopy and found that TcaP is an external scaffold, that is functionally and somewhat structurally similar to the external scaffold, Sid, encoded by the unrelated satellite P4 (2). Finally, we showed that TcaP is largely conserved across PLEs. Together, these data support a model in which TcaP directs the assembly of small capsids comprised of ICP1 coat proteins, which inhibits the complete packaging of the ICP1 genome and permits more efficient packaging of replicated PLE genomes.

PubMed: 36909475
DOI: 10.1101/2023.03.01.530633

Experimental method

ELECTRON MICROSCOPY (3.4 Å)