ArticleProceedings of the National Academy of Sciences of the United States of America2015
CryoEM and mutagenesis reveal that the smallest capsid protein cements and stabilizes Kaposi's sarcoma-associated herpesvirus capsid.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- The Kaposi's sarcoma-associated herpesvirus viral genome packaging accessory factor ORF68 forms cytoplasmic puncta dependent on the viral tyrosine kinase.bioRxiv : the preprint server for biology · 2026Article
- Article
- A Capsid Structure ofViruses · 2022Article
- Article
- The Ins and Outs of Herpesviral Capsids: Divergent Structures and Assembly Mechanisms across the Three Subfamilies.Viruses · 2021Review
- Cryo-EM structure of the varicella-zoster virus A-capsid.Nature communications · 2020Article
- Structure of the herpes simplex virus type 2 C-capsid with capsid-vertex-specific component.Nature communications · 2018Article
- A Hyperthermophilic Phage Decoration Protein Suggests Common Evolutionary Origin with Herpesvirus Triplex Proteins and an Anti-CRISPR Protein.Structure (London, England : 1993) · 2018Article
- Structure of the herpes simplex virus 1 capsid with associated tegument protein complexes.Science (New York, N.Y.) · 2018Article
- Novel Role of vBcl2 in the Virion Assembly of Kaposi's Sarcoma-Associated Herpesvirus.Journal of virology · 2018Article
- Structure and mutagenesis reveal essential capsid protein interactions for KSHV replication.Nature · 2018Article
- Functional Carboxy-Terminal Fluorescent Protein Fusion to Pseudorabies Virus Small Capsid Protein VP26.Journal of virology · 2018Article
- A pUL25 dimer interfaces the pseudorabies virus capsid and tegument.The Journal of general virology · 2017Article
- Virus-Like Vesicles of Kaposi's Sarcoma-Associated Herpesvirus Activate Lytic Replication by Triggering Differentiation Signaling.Journal of virology · 2017Article
- Atomic structure of the human cytomegalovirus capsid with its securing tegument layer of pp150.Science (New York, N.Y.) · 2017Article
- Incorporation of the Kaposi's sarcoma-associated herpesvirus capsid vertex-specific component (CVSC) into self-assembled capsids.Virus research · 2017Article
- Reactivation and Lytic Replication of Kaposi's Sarcoma-Associated Herpesvirus: An Update.Frontiers in microbiology · 2017Review
- HVint: A Strategy for Identifying Novel Protein-Protein Interactions in Herpes Simplex Virus Type 1.Molecular & cellular proteomics : MCP · 2016Article
- Extensive subunit contacts underpin herpesvirus capsid stability and interior-to-exterior allostery.Nature structural & molecular biology · 2016Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 4 countries.
Funding
Abstract
With just one eighth the size of the major capsid protein (MCP), the smallest capsid protein (SCP) of human tumor herpesviruses--Kaposi's sarcoma-associated herpesvirus (KSHV) and Epstein-Barr virus (EBV)--is vital to capsid assembly, yet its mechanism of action is unknown. Here, by cryoEM of KSHV at 6-Å resolution, we show that SCP forms a crown on each hexon and uses a kinked helix to cross-link neighboring MCP subunits. SCP-null mutation decreased viral titer by 1,000 times and impaired but did not fully abolish capsid assembly, indicating an important but nonessential role of SCP. By truncating the C-terminal half of SCP and performing cryoEM reconstruction, we demonstrate that SCP's N-terminal half is responsible for the observed structure and function whereas the C-terminal half is flexible and dispensable. Serial truncations further highlight the critical importance of the N-terminal 10 aa, and cryoEM reconstruction of the one with six residues truncated localizes the N terminus of SCP in the cryoEM density map and enables us to construct a pseudoatomic model of SCP. Fitting of this SCP model and a homology model for the MCP upper domain into the cryoEM map reveals that SCP binds MCP largely via hydrophobic interactions and the kinked helix of SCP bridges over neighboring MCPs to form noncovalent cross-links. These data support a mechanistic model that tumor herpesvirus SCP reinforces the capsid for genome packaging, thus acting as a cementing protein similar to those found in many bacteriophages.
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