Expression and characterization of virus-like particles containing rubella virus structural proteins

Qiu, Zhiyong; Ou, Dawei; Hobman, Tom C.; Gillam, Shirley

doi:10.1128/jvi.68.6.4086-4091.1994

Cited by 42 publications

(25 citation statements)

References 44 publications

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“…First, replicons which express only the nonstructural proteins and replicate the replicon RNA (Tzeng et al, 2001) can be used to determined if the nonstructural proteins and the process of RNA replication is sufficient for attracting the RER, mitochondria, and Golgi to the CVs. Second, it has been found that expression of structural proteins results in formation of virus-like particles (VLPs) that are similar in all aspects, including morphology, to virions Qiu et al, 1994). While VLPs do not contain genome RNA, it is not unequivocally clear whether they incorporate cellular RNA molecules.…”

Section: Discussionmentioning

confidence: 99%

Structural maturation of rubella virus in the Golgi complex

2003

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Rubella virus is a small enveloped virus that assembles in association with Golgi membranes. Freeze-substitution electron microscopy of rubella virus-infected cells revealed a previously unrecognized virion polymorphism inside the Golgi stacks: homogeneously dense particles without a defined core coexisting with less dense, mature virions that contained assembled cores. The homogeneous particles appear to be a precursor form during the virion morphogenesis process as the forms with mature morphology were the only ones detected inside secretory vesicles and on the exterior of cells. In mature virions potential remnants of C protein membrane insertion were visualized as dense strips connecting the envelope with the internal core. In infected cells Golgi stacks were frequently seen close to cytopathic vacuoles, structures identified as the sites for viral RNA replication, along with the rough endoplasmic reticulum and mitochondria. These associations could facilitate the transfer of viral genomes from the cytopathic vacuoles to the areas of rubella assembly in Golgi membranes.

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Section: Discussionmentioning

confidence: 99%

Structural maturation of rubella virus in the Golgi complex

2003

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“…Of particular significance is the development of cDNA constructs that express RV structural proteins that assemble into rubella virus-like particles (RLP). These RLPs have similar morphology and sites of budding to their wild-type counterpart, and they serve as a convenient tool in dissecting the RV assembly pathway (58,126). For RV, the assembly of structural proteins begins immediately following translation of these proteins.…”

Section: Structural Proteins: Translation Processing and Assemblymentioning

confidence: 99%

“…The role of the capsid protein in RV assembly is less well defined. It has been proposed that maintenance of the E2 signal sequence as part of the capsid protein after cleavage allows the capsid protein to be transported along with the glycoproteins to the Golgi complex (126). Earlier studies postulated that the interaction of the E1 cytoplasmic domain and the RV capsid protein triggered virus budding (58).…”

Section: Structural Proteins: Translation Processing and Assemblymentioning

confidence: 99%

Rubella Virus Replication and Links to Teratogenicity

2000

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SUMMARY Rubella virus (RV) is the causative agent of the disease known more popularly as German measles. Rubella is predominantly a childhood disease and is endemic throughout the world. Natural infections of rubella occur only in humans and are generally mild. Complications of rubella infection, most commonly polyarthralgia in adult women, do exist; occasionally more serious sequelae occur. However, the primary public health concern of RV infection is its teratogenicity. RV infection of women during the first trimester of pregnancy can induce a spectrum of congenital defects in the newborn, known as congenital rubella syndrome (CRS). The development of vaccines and implementation of vaccination strategies have substantially reduced the incidence of disease and in turn of CRS in developed countries. The pathway whereby RV infection leads to teratogenesis has not been elucidated, but the cytopathology in infected fetal tissues suggests necrosis and/or apoptosis as well as inhibition of cell division of critical precursor cells involved in organogenesis. In cell culture, a number of unusual features of RV replication have been observed, including mitochondrial abnormalities, and disruption of the cytoskeleton; these manifestations are most probably linked and play some role in RV teratogenesis. Further understanding of the mechanism of RV teratogenesis will be brought about by the investigation of RV replication and virus-host interactions.

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“…These posttranslational events in antigen formation may be particularly important in the synthesis of envelope glycoprotein structures, especially those that are heterodimeric. Production of recombinant DNA-derived viral surface proteins in a viruslike particulate form using eukaryotic cells has been reported for several enveloped viruses (1,4,5,26,27,(31)(32)(33). Since virion maturation may be driven by the ability of the individual envelope proteins to self-assemble, some viral proteins may self-assemble and be released from cells transfected with their genes, greatly facilitating their production and purification.…”

mentioning

confidence: 99%

Generation and Characterization of a Mammalian Cell Line Continuously Expressing Japanese Encephalitis Virus Subviral Particles

Konishi

Fujii

Mason

2001

J Virol

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We have generated a cell line (F cells) producing a secreted form of Japanese encephalitis virus (JEV) subviral particle (extracellular particles [EPs]) that contains the JEV envelope glycoprotein (E) and a precursor (prM) of the virion membrane protein (M). The F cells were engineered to synthesize these JEV products from a cDNA encoding a mutated (furin proteinase resistant) form of prM, since stable cell lines expressing E and the authentic form of prM could not be obtained, due (in part) to the cell-fusing ability of EPs containing E and M. Our biochemical alteration of the prM protein was critical for the successful production of EP-producing cell lines. EPs produced by F cells share the biochemical properties of empty viral particles produced by JEV-infected cells, except that the F-cell EPs lack hemagglutinating activity and M. F-cell EPs were recognized by a panel of monoclonal antibodies to E, and EPs were shown to be useful as vaccine candidates in mice and as diagnostic reagents in evaluating human immune responses to JE vaccination. The amounts of E antigen released into the culture fluid of F cells were similar to those found in virion fractions of JEV-infected cell culture fluids or JEV-infected weanling mouse brains (the current source of antigen used to produce human vaccines for JE). Thus, the F-cell line would appear to be a useful source of antigen for JE vaccines and diagnostics.

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Expression and characterization of virus-like particles containing rubella virus structural proteins

Cited by 42 publications

References 44 publications

Structural maturation of rubella virus in the Golgi complex

Structural maturation of rubella virus in the Golgi complex

Rubella Virus Replication and Links to Teratogenicity

Generation and Characterization of a Mammalian Cell Line Continuously Expressing Japanese Encephalitis Virus Subviral Particles

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