Type D Retrovirus Gag Polyprotein Interacts with the Cytosolic Chaperonin TRiC

Choi, Gyu; Park, Sunyoung; Chung, An‐Sik; Hunter, Eric; Rhee, Sehun

doi:10.1128/jvi.75.6.2526-2534.2001

Cited by 59 publications

(48 citation statements)

References 57 publications

(51 reference statements)

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“…Mason-Pfizer monkey virus, a b retrovirus, which assembles in pericentriolar clusters, specific chaperones have been implicated in the protein assembly process (Hong et al 2001;Sfakianos et al 2003) and in the case of human immunodeficiency virus, RNase L inhibitor is associated with protein assembly intermediates (Zimmerman et al 2002). Nonetheless, relatively little is known about which, if any, host factors might play a specific role in directing genomic RNA into the assembly rather than translation pathway.…”

Section: Resultsmentioning

confidence: 99%

Virus-like particles of the Ty3 retrotransposon assemble in association with P-body components

Beliakova-Bethell¹,

Beckham²,

Giddings³

et al. 2005

RNA

137

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Retroviruses and retrotransposons assemble intracellular immature core particles around a RNA genome, and nascent particles collect in association with membranes or as intracellular clusters. How and where genomic RNA are identified for retrovirus and retrotransposon assembly, and how translation and assembly processes are coordinated is poorly understood. To understand this process, the subcellular localization of Ty3 RNA and capsid proteins and virus-like particles was investigated. We demonstrate that mRNAs, proteins, and virus-like particles of the yeast Ty3 retrotransposon accumulate in association with cytoplasmic P-bodies, which are sites of mRNA translation repression, storage, and degradation. Deletions of genes encoding P-body proteins decreased Ty3 transposition and caused changes in the pattern of Ty3 foci, underscoring the biological significance of the association of Ty3 virus-like protein components and P-bodies. These results suggest the hypothesis that P-bodies may serve to segregate translation and assembly functions of the Ty3 genomic RNA to promote assembly of virus-like particles. Because Ty3 has features of a simple retrovirus and P-body functions are conserved between yeast and metazoan organisms, these findings may provide insights into host factors that facilitate retrovirus assembly.

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Section: Resultsmentioning

confidence: 99%

Virus-like particles of the Ty3 retrotransposon assemble in association with P-body components

Beliakova-Bethell¹,

Beckham²,

Giddings³

et al. 2005

RNA

137

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“…Indeed, one such component (hnRNP A2) has previously been reported to regulate HIV-1 gRNA trafficking and virus production (24). (ii) Retrovirus Gag assembly is a stepwise, energy-dependent process that requires chaperone proteins (13,16,18,55). Therefore, differences in Gag synthesis sites as a consequence of different RNA nuclear export pathways might lead to exposure of Gag to different cellular factors.…”

Section: Discussionmentioning

confidence: 99%

Distinct Intracellular Trafficking of Equine Infectious Anemia Virus and Human Immunodeficiency Virus Type 1 Gag during Viral Assembly and Budding Revealed by Bimolecular Fluorescence Complementation Assays

Jin

Sturgeon²,

Chen

et al. 2007

J Virol

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In rodent cells, Rev-dependent HIV-1 Gag assembly and budding were blocked, but changing RRE to PRE rescued HIV-1 Gag assembly and budding. In contrast, EIAV Gag polyproteins synthesized from mRNA exported via either Rev-dependent or PRE-dependent mechanisms were able to assemble and bud efficiently in rodent cells. Taken together, our results suggest that lentivirus assembly and budding are regulated by the RNA nuclear export pathway and that alternative cellular pathways can be adapted for lentiviral Gag assembly and budding.

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“…The CCT complex has also been implicated in playing a role in the life cycle of several other viruses. For example, it is involved in folding of newly synthesized Gag polyproteins of Mason-Pfitzer monkey virus (M-PMV) (23). CCT also plays a role in viral assembly of hepatitis B virus (35) and initial folding of EBNA-3 nuclear protein of Epstein-Barr virus (31).…”

Section: Discussionmentioning

confidence: 99%

Association of the Influenza Virus RNA Polymerase Subunit PB2 with the Host Chaperonin CCT

Fislová

Thomas

Graef

et al. 2010

J Virol

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The RNA polymerase of influenza A virus is a host range determinant and virulence factor. In particular, the PB2 subunit of the RNA polymerase has been implicated as a crucial factor that affects cell tropism as well as virulence in animal models. These findings suggest that host factors associating with the PB2 protein may play an important role during viral replication. In order to identify host factors that associate with the PB2 protein, we purified recombinant PB2 from transiently transfected mammalian cells and identified copurifying host proteins by mass spectrometry. We found that the PB2 protein associates with the cytosolic chaperonin containing TCP-1 (CCT), stress-induced phosphoprotein 1 (STIP1), FK506 binding protein 5 (FKBP5), ␣-and ␤-tubulin, Hsp60, and mitochondrial protein p32. Some of these binding partners associate with each other, suggesting that PB2 might interact with these proteins in multimeric complexes. More detailed analysis of the interaction of the PB2 protein with CCT revealed that PB2 associates with CCT as a monomer and that the CCT binding site is located in a central region of the PB2 protein. PB2 proteins from various influenza virus subtypes and origins can associate with CCT. Silencing of CCT resulted in reduced viral replication and reduced PB2 protein and viral RNA accumulation in a ribonucleoprotein reconstitution assay, suggesting an important function for CCT during the influenza virus life cycle. We propose that CCT might be acting as a chaperone for PB2 to aid its folding and possibly its incorporation into the trimeric RNA polymerase complex.Influenza A viruses, members of the family of Orthomyxoviridae, contain a segmented RNA genome of negative polarity. The genomic RNA segments together with the three subunits of the viral RNA-dependent RNA polymerase (PB1, PB2, and PA protein) and the nucleoprotein (NP) form viral ribonucleoprotein complexes (vRNPs). The PB1 subunit is the polymerase itself, while the PB2 and PA subunits are involved in the generation of 5Ј capped RNA primers through binding to and endonucleolytic cleavage of host pre-mRNAs (8,10,11,41,61). After the virus enters the cell via endocytosis, vRNPs are released into the cytoplasm and transported into the nucleus. In the nucleus, vRNPs catalyze the synthesis of viral mRNAs and complementary RNAs (cRNA) which, in turn, are used as templates for the synthesis of vRNAs. The newly formed vRNPs in association with other viral proteins (M1 and nonstructural protein 2/nuclear export factor [NS2/NEP]) are transported into the cytoplasm and subsequently to the cell membrane, where the assembly process takes place, followed by the release of progeny virions by budding (44).The PB1, PB2, and PA proteins are synthesized in the cytoplasm whereupon PB1 and PA form a dimeric complex that is transported into the nucleus. In the nucleus the dimer assembles with the PB2 subunit, which is transported separately (7,14). RanBP5 was identified as a factor that is involved in the import of the PB1-PA dimer into the nucleus ...

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Type D Retrovirus Gag Polyprotein Interacts with the Cytosolic Chaperonin TRiC

Cited by 59 publications

References 57 publications

Virus-like particles of the Ty3 retrotransposon assemble in association with P-body components

Virus-like particles of the Ty3 retrotransposon assemble in association with P-body components

Distinct Intracellular Trafficking of Equine Infectious Anemia Virus and Human Immunodeficiency Virus Type 1 Gag during Viral Assembly and Budding Revealed by Bimolecular Fluorescence Complementation Assays

Association of the Influenza Virus RNA Polymerase Subunit PB2 with the Host Chaperonin CCT

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