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- PDB-8g1r: A Vibrio cholerae viral satellite enables efficient horizontal tr... -

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Basic information

Entry
Database: PDB / ID: 8g1r
TitleA Vibrio cholerae viral satellite enables efficient horizontal transfer by using an external scaffold to assemble hijacked coat proteins into small capsids
Components
  • Serine protease
  • major head protein
KeywordsVIRUS LIKE PARTICLE / PLE / Procapsid
Function / homologyMajor capsid protein GpE / Phage major capsid protein E / host cell cytoplasm / Putative major head protein / Phage protein
Function and homology information
Biological speciesVibrio phage ICP1_2011_A (virus)
Vibrio cholerae (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsSubramanian, S. / Boyd, C.M. / Seed, K.D. / Parent, K.N.
Funding support United States, 6items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM110185 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM116789 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM140803 United States
National Science Foundation (NSF, United States)1750125 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI127652 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI127652 United States
Citation
Journal: bioRxiv / Year: 2023
Title: A viral satellite maximizes its spread and inhibits phage by remodeling hijacked phage coat proteins into small capsids.
Authors: Caroline M Boyd / Sundharraman Subramanian / Drew T Dunham / Kristin N Parent / Kimberley D Seed /
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 ...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.
#1: Journal: Elife / Year: 2024
Title: A viral satellite maximizes its spread and inhibits phage by remodeling hijacked phage coat proteins into small capsids.
Authors: Caroline M Boyd / Sundharraman Subramanian / Drew T Dunham / Kristin N Parent / Kimberley D Seed /
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 ...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 , phage-inducible chromosomal island-like element (PLE), remodels the capsid it has been predicted to steal from the phage ICP1 (Netter et al., 2021). 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 bona fide 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 (Kizziah et al., 2020). 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.
History
DepositionFeb 2, 2023Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 17, 2024Provider: repository / Type: Initial release
Revision 1.1Jan 24, 2024Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Oct 16, 2024Group: Data collection / Database references / Structure summary
Category: citation / citation_author ...citation / citation_author / em_admin / pdbx_entry_details
Item: _em_admin.last_update

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: major head protein
B: major head protein
C: major head protein
D: major head protein
E: Serine protease


Theoretical massNumber of molelcules
Total (without water)186,9435
Polymers186,9435
Non-polymers00
Water00
1
A: major head protein
B: major head protein
C: major head protein
D: major head protein
E: Serine protease
x 60


Theoretical massNumber of molelcules
Total (without water)11,216,595300
Polymers11,216,595300
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation59
2


  • Idetical with deposited unit
  • icosahedral asymmetric unit
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
A: major head protein
B: major head protein
C: major head protein
D: major head protein
E: Serine protease
x 5


  • icosahedral pentamer
  • 935 kDa, 25 polymers
Theoretical massNumber of molelcules
Total (without water)934,71625
Polymers934,71625
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation4
4
A: major head protein
B: major head protein
C: major head protein
D: major head protein
E: Serine protease
x 6


  • icosahedral 23 hexamer
  • 1.12 MDa, 30 polymers
Theoretical massNumber of molelcules
Total (without water)1,121,65930
Polymers1,121,65930
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation5
5


  • Idetical with deposited unit
  • icosahedral asymmetric unit, std point frame
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
SymmetryPoint symmetry: (Schoenflies symbol: I (icosahedral))

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Components

#1: Protein
major head protein / Coat


Mass: 38428.023 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Vibrio phage ICP1_2011_A (virus) / Gene: ICP12011A_121 / Plasmid: pETDUET / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: A0A385IH56
#2: Protein Serine protease


Mass: 33231.152 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Vibrio cholerae (bacteria) / Strain: El Tor / Variant: PLE1 / Plasmid: pETDUET / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: M1R2Y9
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: PLE Procapsid / Type: COMPLEX / Entity ID: all / Source: MULTIPLE SOURCES
Molecular weightExperimental value: NO
Source (natural)Organism: Vibrio cholerae (bacteria) / Strain: El Tor
Source (recombinant)Organism: Escherichia coli BL21 (bacteria) / Plasmid: pETDUET
Details of virusEmpty: NO / Enveloped: NO / Isolate: OTHER / Type: VIRION
Natural hostOrganism: Shigella flexneri Y
Buffer solutionpH: 7.5
Details: 50 mM Tris-HCl, pH 7.4, 100 mM NaCl, 10 mM MgSO4, 1 mM CaCl2
Buffer component
IDConc.NameFormulaBuffer-ID
150 mMtris(hydroxymethyl)aminomethane hydrochlorideC4H11NO3-HCl1
2100 mMsodium chlorideNaCl1
310 mMmagnesium sulfateMgSO41
41 mMcalcium chlorideCaCl21
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 277.15 K

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 700 nm
Image recordingElectron dose: 36.41 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

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Processing

CTF correctionType: NONE
SymmetryPoint symmetry: I (icosahedral)
3D reconstructionResolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 379643 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00310070
ELECTRON MICROSCOPYf_angle_d0.52513777
ELECTRON MICROSCOPYf_dihedral_angle_d4.2281542
ELECTRON MICROSCOPYf_chiral_restr0.041679
ELECTRON MICROSCOPYf_plane_restr0.0041800

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