Intracellular transport of rubella virus structural proteins expressed from cloned cDNA

Baron, Michael D.; Ebel, Thomas; Suomalainen, Maarit

doi:10.1099/0022-1317-73-5-1073

Cited by 31 publications

(42 citation statements)

References 71 publications

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“…The p110 protein is translocated into the ER by two separate signal peptides, 23 and 20 amino acids in length, located at the amino termini of E2 and E1, respectively. Within the ER, the RV capsid protein is cleaved from E2 and E2 is cleaved from E1 (10,24,36,92,137). Unlike the alphaviruses, where an autoprotease cleaves the alphavirus capsid protein from the polyprotein precursor, cleavage of RV capsid protein is mediated by a cellular signalase found within the lumen of the ER (24,36).…”

Section: Structural Proteins: Translation Processing and Assemblymentioning

confidence: 99%

Rubella Virus Replication and Links to Teratogenicity

Lee

Bowden

2000

Clinical Microbiology Reviews

152

115

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Section: Structural Proteins: Translation Processing and Assemblymentioning

confidence: 99%

Rubella Virus Replication and Links to Teratogenicity

Lee

Bowden

2000

Clinical Microbiology Reviews

152

115

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“…In cells transiently expressing all three structural proteins, a pool of capsid is localized to the Golgi region, where budding of virions typically occurs (4,22,39). In the absence of E2 and E1, capsid has been reported to associate largely with the endoplasmic reticulum (4). Subsequently, immunogold electron microscopy and indirect immunofluorescence studies revealed that pools of capsid are also associated with mitochondria and viral replication complexes (6,35).…”

mentioning

confidence: 99%

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confidence: 99%

Interactions between Rubella Virus Capsid and Host Protein p32 Are Important for Virus Replication

Beatch

Everitt²,

Law³

et al. 2005

J Virol

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The distribution and morphology of mitochondria are dramatically affected during infection with rubella virus (RV). Expression of the capsid, in the absence of other viral proteins, was found to induce both perinuclear clustering of mitochondria and the formation of electron-dense intermitochondrial plaques, both hallmarks of RV-infected cells. We previously identified p32, a host cell mitochondrial matrix protein, as a capsid-binding protein. Here, we show that two clusters of arginine residues within capsid are required for stable binding to p32. Mutagenic ablation of the p32-binding site in capsid resulted in decreased mitochondrial clustering, indicating that interactions with this cellular protein are required for capsid-dependent reorganization of mitochondria. Recombinant viruses encoding arginine-to-alanine mutations in the p32-binding region of capsid exhibited altered plaque morphology and replicated to lower titers. Further analysis indicated that disruption of stable interactions between capsid and p32 was associated with decreased production of subgenomic RNA and, consequently, infected cells produced significantly lower amounts of viral structural proteins under these conditions. Together, these results suggest that capsid-p32 interactions are important for nonstructural functions of capsid that include regulation of virus RNA replication and reorganization of mitochondria during infection.

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“…OLinked oligosaccharides are observed only in E2 (Sanchez & Frey, 1991;LundstrSm et al, 1991). Formation of El-E2 heterodimers in the ER (Baron & Forsell, 1991) facilitates the transport of E2 (Hobman et al, 1990) and E1 (Baron et al, 1992;Hobman et al, 1993) to the Golgi complex.…”

Section: Introductionmentioning

confidence: 99%

Brefeldin A and monensin arrest cell surface expression of membrane glycoproteins and release of rubella virus

Qiu¹,

Tufaro

Gillam³

1995

Journal of General Virology

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The maturation of rubella virus (RV) glycoproteins E2 and E1 was examined by using brefeldin A (BFA) and monensin. BFA, which induces the rapid redistribution of Golgi enzymes residing in the Golgi complex into the endoplasmic reticulum (ER), was used to locate the intracellular site for the modification of carbohydrate side-chains on RV E1 and E2 proteins. The monovalent ionophore monensin, which inhibits intracellular transport of proteins through the ER-Golgi complex, was used to block the transport of E1 and E2 glycoproteins through the Golgi complex. BFA and monensin effectively blocked the cell surface expression of RV E2 and El proteins, secretion of an anchor-free form of E2 and budding of RV from the plasma membrane. For Olinked glycosylation, addition of N-acetylgalactosamine and galactose to E2 protein was found to take place in the medial to the trans Golgi. A dramatic change in the intracellular distribution of RV structural proteins was observed when transfected COS cells were treated with BFA or monensin, although the proteolytic processing of RV structural protein precursor was not affected. In the presence of BFA or monensin, virus release from infected Vero cells was only 0.1% of the intracellular virus, and the intracellular virus titre decreased as well. Our results suggest that O-linked glycosylation on the E2 protein occurred in the post-ER region and the transport of RV structural proteins to the Golgi complex and postGolgi compartment may be a rate-limiting step in RV assembly and budding.

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Intracellular transport of rubella virus structural proteins expressed from cloned cDNA

Cited by 31 publications

References 71 publications

Rubella Virus Replication and Links to Teratogenicity

Rubella Virus Replication and Links to Teratogenicity

Interactions between Rubella Virus Capsid and Host Protein p32 Are Important for Virus Replication

Brefeldin A and monensin arrest cell surface expression of membrane glycoproteins and release of rubella virus

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