The role of inter-subunit ionic interactions in the assembly of Physalis mottle tymovirus

@article{Umashankar2006TheRO,
  title={The role of inter-subunit ionic interactions in the assembly of Physalis mottle tymovirus},
  author={Mahadevaiah Umashankar and M. R. V. Murthy and S. Anil Singh and A. G. Appu Rao and Handanahal Subbarao Savithri},
  journal={Archives of Virology},
  year={2006},
  volume={151},
  pages={1917-1931}
}
Summary.Physalis mottle tymovirus (PhMV) is a small spherical plant virus with its RNA genome encapsidated in a protein shell made of 180 identical coat protein (CP) subunits. The amino acid residues involved in two interfacial salt bridges, Asp-83/Arg-159 and Arg-68/Asp-150 and Lys-153, were targeted for mutagenesis with a view to delineate the role of interfacial ionic interactions in the subunit folding and assembly of the virus. R159A and D83A-R159A recombinant CP (rCP) mutants formed… 
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References

SHOWING 1-10 OF 20 REFERENCES
Identification of a discrete intermediate in the assembly/disassembly of physalis mottle tymovirus through mutational analysis.
TLDR
It is demonstrated that the amino-terminal segment is flexible and either the deletion or addition of amino acid residues at the N terminus does not affect T=3 capsid assembly, and the deletion of even a single residue from the C terminus resulted in capsids that were unstable.
Mutation of Interfacial Residues Disrupts Subunit Folding and Particle Assembly of Physalis mottle tymovirus *
TLDR
The mutation of residues involved in inter-subunit interactions in PhMV disrupts both subunit folding and particle assembly as revealed by sucrose density gradient analysis, circular dichroism, fluorescence, thermal, and urea denaturation studies.
Assembly of physalis mottle virus capsid protein in Escherichia coli and the role of amino and carboxy termini in the formation of the icosahedral particles.
TLDR
Results demonstrate that the N-terminal 26 amino acid residues are not essential for T=3 capsid assembly in PhMV, and suggest that these residues are crucial for folding and assembly of the particles.
Three-dimensional structure of physalis mottle virus: implications for the viral assembly.
TLDR
Comparison of PhMV with the sobemovirus, sesbania mosaic virus reveals striking similarities in the overall tertiary fold of the coat protein although the capsid morphologies of these two viruses are very different.
Structural studies on the empty capsids of Physalis mottle virus.
TLDR
The three-dimensional crystal structure of the empty capsid of Physalis mottle tymovirus has been determined and encapsidation of RNA appears to cause a reduction in the particle radius concomittant with the ordering of the N-terminal arm in the three subunits.
Poliovirus assembly and encapsidation of genomic RNA.
In vitro expression of belladonna mottle virus genome.
TLDR
In vitro translation of belladonna mottle virus BDMV(I) genomic RNA in a rabbit reticulocyte lysate system produced proteins which form the non-structural proteins and the coat protein was expressed from a subgenomic RNA which was found to be encapsidated in the empty capsids forming the top component viral particles.
Evidence for the existence of a coat protein messenger RNA associated with the top component of each of three tymoviruses.
TLDR
On centrifugation in a CsCl density gradient the three tymoviruses, eggplant mosaic, wild cucumber mosaic, and okra mosaic, separate into a major bottom component and several less dense minor components, which induced the synthesis of coat protein when translated in wheat-germ and rabbit-reticulocyte cell-free systems.
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