Rotavirus proteins: structure and assembly.

@article{Pesavento2006RotavirusPS,
  title={Rotavirus proteins: structure and assembly.},
  author={Joseph B Pesavento and Sue E. Crawford and Mary K. Estes and B. V. Venkataram Prasad},
  journal={Current topics in microbiology and immunology},
  year={2006},
  volume={309},
  pages={
          189-219
        }
}
Rotavirus is a major pathogen of infantile gastroenteritis. It is a large and complex virus with a multilayered capsid organization that integrates the determinants of host specificity, cell entry, and the enzymatic functions necessary for endogenous transcription of the genome that consists of 11 dsRNA segments. These segments encode six structural and six nonstructural proteins. In the last few years, there has been substantial progress in our understanding of both the structural and… 
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171 Citations
Highly Influential Citations
10
Background Citations
84
Methods Citations
5
Results Citations
1

171 Citations

Molecular Biology of Rotavirus Entry and Replication
TLDR
This paper reviews and tries to integrate the new knowledge about rotavirus entry, replication, and assembly, and poses some of the questions that remain to be solved.
Structural Insights into Rotavirus Entry.
TLDR
This review feeds on the abundant structural information produced for rotavirus during the past 30 years and focuses on the structure and the dynamics of the rotav virus entry machinery.
Assortment and packaging of the segmented rotavirus genome.
Bluetongue virus: dissection of the polymerase complex.
  • P. Roy
  • Biology
    The Journal of general virology
  • 2008
TLDR
Current understanding of these catalytic proteins as derived from the use of recombinant proteins, combined with functional assays and the in vitro reconstitution of the transcription/replication complex are focused on.
Mechanism of Intraparticle Synthesis of the Rotavirus Double-stranded RNA Genome*
TLDR
The current understanding of rotavirus RNA synthetic mechanisms is reviewed, finding that this intraparticle strategy of RNA synthesis helps orchestrate the concerted packaging and replication of the viral genome.
The basic architecture of viruses.
TLDR
Study of virus structures is required to understand structure-function relationships in viruses, including those related to morphogenesis and antigenicity, and these structural foundations can be extended to other macromolecular complexes that control many fundamental processes in biology.
Reverse genetics systems of segmented double-stranded RNA viruses including rotavirus
TLDR
The replication cycle of rotavirus is described, a general background to the development of rotavirus reverse genetics is provided, and the reverse genetics system for dsRNA viruses, including rotvirus is summarized.
The picobirnavirus crystal structure provides functional insights into virion assembly and cell entry
TLDR
The structure of a picobirnavirus shows a simple core capsid with a distinctive icosahedral arrangement, displaying 60 two‐fold symmetric dimers of a coat protein (CP) with a new 3D‐fold, and it is shown that, as many non‐enveloped animal viruses, CP undergoes an autoproteolytic cleavage, releasing a post‐translationally modified peptide that remains associated with nucleic acid within the capsid.
Protein disulfide isomerase and heat shock cognate protein 70 interactions with rotavirus structural proteins using their purified recombinant versions
TLDR
An analysis of the interactions between recombinant rotavirus structural proteins VP5*, VP8* and VP6, and cellular proteins Hsc70 and PDI using their purified recombinant versions concludes that rVP5* and rVP6 interact with HSc70 andPDI during the rotav virus infection process.
Challenges for the production of virus-like particles in insect cells: The case of rotavirus-like particles
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References

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TLDR
The X-ray structure of the functional octamer of NSP2 of rotavirus, which exhibits nucleoside triphosphatase, single-stranded RNA binding, and nucleic-acid helix-destabilizing activities, is presented and it is suggested that the nucleotide-binding site is located inside the cleft between the two domains.
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TLDR
It is proposed that the observed organization of the dsRNA is conducive for an orchestrated movement of the RNA relative to the enzyme complex during transcription, as well as the largest amount of icosahedrally ordered RNA observed in any virus structure to date.
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TLDR
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TLDR
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TLDR
Analysis of the reovirus core by X-ray crystallography shows that there are alternative, specific and completely non-equivalent contacts made by several surfaces of two of its proteins; that the RNA capping and export apparatus is a hollow cylinder, which probably sequesters its substrate to ensure completion of the capping reactions.
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TLDR
The results obtained strengthen the importance of secondary transcription/translation in rotavirus replication and demonstrate that NSP5 is essential for the assembly of viroplasms and virus replication.
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