Release of virus-like particles from cells infected with poliovirus replicons which express human immunodeficiency virus type 1 Gag

Porter, Donna C.; Melsen, Lawrence R.; Compans, Richard W.; Morrow, Casey D.

doi:10.1128/jvi.70.4.2643-2649.1996

Cited by 21 publications

(7 citation statements)

References 67 publications

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“…In previous studies, we have demonstrated that RNA from poliovirus-based replicon genomes could be encapsidated if transfected into cells previously infected with a recombinant vaccinia virus, VV-P1, which expresses the P1 protein (Ansardi et al, 1994;Porter et al, 1993Porter et al, , 1995Porter et al, , 1996Porter et al, , 1997. Serial passage of encapsidated replicons in VV-P1-infected cells resulted in the generation of stocks of the encapsidated replicon.…”

Section: Encapsidation Of the Replicon Encoding Luciferasementioning

confidence: 99%

“…Cell monolayers of HeLa T4, BSC-40, or HeLa H1 cells (obtained from ATCC) were grown in DMEM supplemented with 10% fetal bovine serum (Porter et al, 1995(Porter et al, , 1996. The recombinant vaccinia virus, VV-P1, which expresses the P1 capsid precursor protein in infected cells has been previously described (Ansardi et al, 1991;Morrow et al, , 1995Morrow et al, , 1996a.…”

Section: Tissue Culture Cells and Virusesmentioning

confidence: 99%

“…Previous studies from this laboratory have described the encapsidation and serial passage of replicon genomes containing foreign gene sequences using the recombinant vaccinia virus VV-P1 to provide P1 in trans (Porter et al, 1993(Porter et al, , 1995(Porter et al, , 1996(Porter et al, , 1997. To encapsidate the replicon RNA, HeLa T4 cells were infected with 5 PFU/ cell of VV-P1, which expresses the poliovirus capsid precursor protein P1 (Ansardi et al, 1991).…”

Section: Encapsidation Of Repliconsmentioning

confidence: 99%

“…Follow-up studies demonstrated that insertion of foreign genes into the P1 region resulted in expression as long as the translational reading frame was maintained between the foreign gene and the poliovirus P2 and P3 regions. Previous studies from this laboratory have described the construction of self-replicating genomes, termed replicons, which encode the nonstructural proteins of poliovirus downstream from a foreign gene substituted for the P1 region (Porter et al, 1993(Porter et al, , 1995(Porter et al, , 1996(Porter et al, , 1997Ansardi et al, 1994;Moldoveanu et al, 1995;Anderson et al, 1996a,b). The transfection of the replicon RNA into cells resulted in replication and expression of the gene substituted for the P1 region.…”

Section: Introductionmentioning

confidence: 99%

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Demonstration of the Specificity of Poliovirus Encapsidation Using a Novel Replicon which Encodes Enzymatically Active Firefly Luciferase

Porter¹,

Ansardi²,

Wang³

et al. 1998

Virology

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The specificity of poliovirus encapsidation has been studied using a novel chimeric genome in which the gene encoding firefly luciferase has been substituted for the VP2-VP3-VP1 genes of the poliovirus capsid (P1) gene. Transfection of RNA transcribed in vitro from this genome resulted in a VP4-luciferase fusion protein which retained luciferase enzyme activity. Since the detection of enzyme activity was dependent upon replication of the transfected RNA genome, we refer to these genomes as replicons. The replicon encoding luciferase was encapsidated upon transfection of the genomic RNA into cells previously infected with a recombinant vaccinia virus, VV-P1, which encodes the poliovirus type 1 capsid proteins (P1). Infection of cells with each serial passage, followed by analysis of luciferase enzyme activity, revealed that encapsidated replicons could be detected at the first passage with VV-P1. Amplification of the titer of encapsidated replicons occurred upon serial passage with VV-P1, as evidenced by the high expression levels of luciferase enzyme activity following infection. Serial passage of the luciferase replicons with poliovirus type 1, 2, or 3 resulted in the trans encapsidation into the type 1, 2, or 3 capsids, respectively. In contrast, serial passage with bovine enterovirus, Coxsackievirus A21 or B3, or enterovirus 70 did not result in trans encapsidation, even though co-infection of cells with the replicon and different enteroviruses resulted in high-level expression of luciferase. The results of this study highlight the specificity of poliovirus encapsidation and point to the use of encapsidated replicons encoding luciferase as a reagent for dissecting elements of replication and encapsidation.

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Section: Encapsidation Of the Replicon Encoding Luciferasementioning

confidence: 99%

Section: Tissue Culture Cells and Virusesmentioning

confidence: 99%

Section: Encapsidation Of Repliconsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Demonstration of the Specificity of Poliovirus Encapsidation Using a Novel Replicon which Encodes Enzymatically Active Firefly Luciferase

Porter¹,

Ansardi²,

Wang³

et al. 1998

Virology

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“…One approach to the development of HIV vaccines is the use of live-virus or bacterial vectors for the in vivo expression of lentivirus gene products (1,11,19,20,26,38,40,41,43). For example, strategies priming with recombinant vaccinia virus or canarypox virus vectors expressing HIV immunogens followed by booster inoculations with glycoprotein or peptides have been tested in primate HIV or simian immunodeficiency virus (SIV) challenge models.…”

mentioning

confidence: 99%

Humoral, mucosal, and cellular immunity in response to a human immunodeficiency virus type 1 immunogen expressed by a Venezuelan equine encephalitis virus vaccine vector

Caley

Betts

Irlbeck

et al. 1997

J Virol

111

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A molecularly cloned attenuated strain of Venezuelan equine encephalitis virus (VEE) has been genetically configured as a replication-competent vaccine vector for the expression of heterologous viral proteins (N. L. Davis, K. W. Brown, and R. E. Johnston, J. Virol. 70:3781-3787, 1996). The matrix/capsid (MA/CA) coding domain of human immunodeficiency virus type 1 (HIV-1) was cloned into the VEE vector to determine the ability of a VEE vector to stimulate an anti-HIV immune response in mice. The VEE-MA/CA vector replicated rapidly in the cytoplasm of baby hamster kidney (BHK) cells and expressed large quantities of antigenically identifiable MA/CA protein. When injected subcutaneously into BALB/c mice, the vector invaded and replicated in the draining lymphoid tissues, expressing HIV-1 MA/CA at a site of potent immune activity. Anti-MA/CA immunoglobulin G (IgG) and IgA antibodies were present in serum of all immunized mice, and titers increased after a second booster inoculation. IgA antibodies specific for MA/CA were detected in vaginal washes of mice that received two subcutaneous immunizations. Cytotoxic T-lymphocyte responses specific for MA/CA were detected following immunization with the MA/CA-expressing VEE vector. These findings demonstrate the ability of a VEE-based vaccine vector system to stimulate a comprehensive humoral and cellular immune response. The multifaceted nature of this response makes VEE an attractive vaccine for immunization against virus infections such as HIV-1, for which the correlates of protective immunity remain unclear, but may include multiple components of the immune system.

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Expression of Human Immunodeficiency Virus Type 1 Gag Protein Precursor and Envelope Proteins from a Vesicular Stomatitis Virus Recombinant: High-Level Production of Virus-like Particles Containing HIV Envelope

et al. 2000

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Recombinant vesicular stomatitis viruses have been developed as high-level expression vectors which serve as effective vaccine vectors in animals (Roberts et al., 1998, J. Virol. 72, 4704-4711; Roberts et al., 1999, J. Virol. 73, 3723-3732). Here we show that two genes can be expressed simultaneously from a single, live-attenuated VSV recombinant. The genes used encode the Pr55(gag) protein precursor of HIV-1 (1.7-kb gene) and an HIV-1 envelope (Env) protein (2.4 kb gene). Our results show that VSV can accommodate up to a 40% increase in genome size with only a threefold reduction in virus titer. Recombinants expressing the Pr55(gag) protein precursor with or without Env protein produced abundant HIV virus-like particles (VLPs) in addition to bullet-shaped VSV particles. HIV Env protein expressed from a VSV recombinant also expressing Gag was specifically incorporated into the HIV VLPs but not into the VSV particles. In contrast, VSV G protein was found in both VSV particles and in HIV VLPs. Such VSV/HIV recombinants producing HIV VLPs with Env protein could be an effective source of HIV-like particles inducing both cellular and antibody-mediated immunity to HIV-1.

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Release of virus-like particles from cells infected with poliovirus replicons which express human immunodeficiency virus type 1 Gag

Cited by 21 publications

References 67 publications

Demonstration of the Specificity of Poliovirus Encapsidation Using a Novel Replicon which Encodes Enzymatically Active Firefly Luciferase

Demonstration of the Specificity of Poliovirus Encapsidation Using a Novel Replicon which Encodes Enzymatically Active Firefly Luciferase

Humoral, mucosal, and cellular immunity in response to a human immunodeficiency virus type 1 immunogen expressed by a Venezuelan equine encephalitis virus vaccine vector

Expression of Human Immunodeficiency Virus Type 1 Gag Protein Precursor and Envelope Proteins from a Vesicular Stomatitis Virus Recombinant: High-Level Production of Virus-like Particles Containing HIV Envelope

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