Closterovirus encoded HSP70 homolog and p61 in addition to both coat proteins function in efficient virion assembly.

  title={Closterovirus encoded HSP70 homolog and p61 in addition to both coat proteins function in efficient virion assembly.},
  author={Tatineni Satyanarayana and Siddarame Gowda and Munir Mawassi and M R Albiach-Mart{\'i} and Mar{\'i}a A. Ayll{\'o}n and Cecile J. Robertson and Stephen M. Garnsey and William O. Dawson},
  volume={278 1},
Assembly of the viral genome into virions is a critical process of the virus life cycle often defining the ability of the virus to move within the plant and to be transmitted horizontally to other plants. Closteroviridae virions are polar helical rods assembled primarily by a major coat protein, but with a related minor coat protein at one end. The Closteroviridae is the only virus family that encodes a protein with similarity to cellular chaperones, a 70-kDa heat-shock protein homolog (HSP70h… 

Closterovirus bipolar virion: evidence for initiation of assembly by minor coat protein and its restriction to the genomic RNA 5' region.

The long flexuous virions of the Closteroviridae have a unique bipolar architecture incorporating two coat proteins, with most of the helical nucleocapsid encapsidated by the major coat protein (CP)

The 64-Kilodalton Capsid Protein Homolog of Beet Yellows Virus Is Required for Assembly of Virion Tails

The dual function of p64 in tail assembly and BYV motility is revealed and the concept of the virion tail as a specialized device for BYV cell-to-cell movement is supported.

Cell‐to‐cell movement and assembly of a plant closterovirus: roles for the capsid proteins and Hsp70 homolog

A dual role for the viral molecular chaperone Hsp70h in virion assembly and transport, combined with the previous finding of this protein in intercellular channels, allowed this work to propose a model of closteroviral movement from cell to cell.

Complex molecular architecture of beet yellows virus particles.

Closteroviruses possess exceptionally long filamentous virus particles that mediate protection and active transport of the genomic RNA within infected plants. These virions are composed of a long

HSP70 and Its Cochaperone CPIP Promote Potyvirus Infection in Nicotiana benthamiana by Regulating Viral Coat Protein Functions

CPIP and HSP70 are crucial components of a distinct translation activity that is associated with potyvirus replication, and CPIP-mediated delivery of CP to HSP 70 promoted CP degradation by increasing its ubiquitination when assayed in the absence of virus infection.

Closteroviruses: Molecular Biology, Evolution and Interactions with Cells

The genome expression of closteroviruses occurs by proteolytic processing and +1 ribosomal frameshifting for the replication-associated products of the 5′ -proximal genes, whereas the 3′-terminal genes are expressed via a nested set of subgenomic mRNAs, which strikingly resembles the expression strategy of nidovirus.

Chaperone-mediated in vitro assembly of Polyomavirus capsids

Polyomavirus capsid assembly can be recapitulated with high-fidelity in vitro using either prokaryotic or eukaryotic hsp70 chaperone systems, thereby supporting a role for cellular chaperones in the in vivo regulation of virion assembly.



HSP70 homolog functions in cell-to-cell movement of a plant virus.

It is demonstrated that the virus-specific member of the HSP70 family of molecular chaperones functions in intercellular translocation and represents an additional type of a plant viral-movement protein.

Interaction between HSP70 homolog and filamentous virions of the Beet yellows virus.

It is demonstrated that HSP70h forms a physical complex with BYV virions, which is stable at high concentrations of sodium chloride; its dissociation using sodium dodecyl sulfate, lithium chloride, or alkaline pH was accompanied by virion disassembly.

Association of heat shock protein 70 with enterovirus capsid precursor P1 in infected human cells

The finding that HSP70 was associated with the capsid precursors of at least two enteroviruses may suggest a functional role of these complexes in the viral life cycles.

The beet yellows closterovirus p65 homologue of HSP70 chaperones has ATPase activity associated with its conserved N-terminal domain but does not interact with unfolded protein chains.

The positive-strand RNA genome of beet yellows closterovirus (BYV) encodes a 65 kDa protein related to the HSP70 family of cell chaperones, which may have a distinct substrate specificity and function in BYV-infected cells.

"Rattlesnake" structure of a filamentous plant RNA virus built of two capsid proteins.

A 75-nm segment at one end of the 1370-nm filamentous viral particle was found to be consistently labeled with both types of antibodies, thus indicating that p24 is indeed the second capsid protein and that the closterovirus particle, unlike those of other plant viruses with helical symmetry, has a "rattlesnake" rather than uniform structure.

In vivo and in vitro association of hsc70 with polyomavirus capsid proteins.

The polyomavirus capsid proteins associate with hsc70 during virus infection as well as in recombinant protein expression systems, which may play a role in preventing the premature assembly of capsids in the cytosol and/or in facilitating the nuclear transport of capsid protein complexes.

Genes Required for Replication of the 15.5-Kilobase RNA Genome of a Plant Closterovirus

A full-length cDNA clone of beet yellows closterovirus (BYV) was engineered and used to map functions involved in the replication of the viral RNA genome and subgenomic RNA formation and the papain-like leader proteinase encoded in the 5′-proximal region of ORF 1a was found to have a dual function in genome amplification.

Lettuce infectious yellows virus: in vitro acquisition analysis using partially purified virions and the whitefly Bemisia tabaci.

Virions of lettuce infectious yellows virus (LIYV; genus Crinivirus) were purified from LIYV-infected plants and their protein composition was analysed by SDS-PAGE and immunoblotting. Virion

The p20 gene product of Citrus tristeza virus accumulates in the amorphous inclusion bodies.

Accumulation of high levels of p20 protein in infected tissue, specific localization of the p20-GFP fusion protein, immunolocalization of p 20 protein into amorphous inclusions, and strong homologous p20protein-p20 protein interactions in the yeast-two-hybrid assay suggest that the p21 protein of CTV is a major component of the areorphous inclusion bodies present in CTV-infected cells.

Diverse groups of plant RNA and DNA viruses share related movement proteins that may possess chaperone-like activity.

Based on the analogy to HSP90, it is speculated that many plant virus movement proteins may mediate virus transport in a chaperone-like manner.