Production of human immunodeficiency virus (HIV)-like particles from cells infected with recombinant vaccinia viruses carrying the gag gene of HIV

Shioda, Tatsuo; Shibuta, Hiroshi

doi:10.1016/0042-6822(90)90194-v

Cited by 122 publications

(82 citation statements)

References 39 publications

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“…Although several studies on the expression of the HIV gag gene in recombinant vaccinia viruses have been reported (7,10,13,16,17,33), only a report by Hu et al (13) described the immunological potency of the recombinants. They constructed 5 recombinants, in which v-gag 1 and v-gag 4 were similar to our vac-gag/pol and vac-gag, respectively.…”

Section: Discussionmentioning

confidence: 99%

“…Ara-C selectively inhibits the growth of vaccinia virus by inhibiting the synthesis of vaccinia virus late proteins while allowing expression of 7.5 K promoter-driven foreign genes (5). The cell lysates were electrophoresed on sodium dodecylsulfate-10% polyacrylamide gel electrophoresis (SDS-PAGE) (18), then polypeptides were electrically transferred to polyvinylidene difluoride filters as previously described (33,39). The filters were reacted with serum of an AIDS patient at a dilution of 1: 100.…”

Section: Methodsmentioning

confidence: 99%

“…The primary product of the gag gene is the p55 gag precursor, which is processed into p17, p24 and p15 mature gag proteins by the protease encoded by the pol gene (25). Several workers have already succeeded in expressing HIV gag proteins in mammalian cells using recombinant vaccinia vectors (7,10,13,16,17,33) and recent reports showed that recombinant vaccinia viruses carrying the gag gene can produce HIV-like particles in mammalian cells (13,16,33). However, only a little is known about the immunological potency of these recombinant vaccinia viruses.…”

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confidence: 99%

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Immune Response of Mice Infected with Recombinant Vaccinia Viruses Carrying the HIV gag Gene

Sugata

Aoki

Shioda

et al. 1991

Microbiology and Immunology

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We examined mouse immune response to 4 kinds of recombinant vaccinia viruses carrying the HIV gag gene, including vac-gag/pol, which produces HIV-like particles with processed gag proteins; vac-gag, which also produces HIV-like particles but with unprocessed gag protein; and vac-gag-pol-fuse and vac-es-gag/pol, neither of which produces such particles but releases reverse transcriptase and gag protein, respectively, from infected cells. Although infection of mice with recombinant vaccinia viruses induced production of the anti-p24 antibody in all mice, vac-gag/pol and vac-es-pol induced higher production than the other two recombinants. Increase in [3H]thymidine uptake by splenic lymphocytes following p24 antigen stimulation was most evident in mice infected with vac-gag/pol. Thus, the highest immune reaction, both humoral and cellular, was elicited by vac-gag/pol, indicating that among those tested, this recombinant vaccinia virus is the best candidate for a vaccine that induces anti-HIV gag immunity.

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Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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confidence: 99%

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Immune Response of Mice Infected with Recombinant Vaccinia Viruses Carrying the HIV gag Gene

Sugata

Aoki

Shioda

et al. 1991

Microbiology and Immunology

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“…Human immunodeficiency virus type 1 (HIV-1) does not require its envelope protein (Env) for virion budding. However, the generated virions were not infectious (Shioda & Shibuta, 1990). Budding of retroviruses seems to occur at ordered lipid microdomains, called lipid rafts (Briggs et al, 2003).…”

Section: Discussionmentioning

confidence: 99%

GP64 of group I nucleopolyhedroviruses cannot readily rescue infectivity of group II f-null nucleopolyhedroviruses

Westenberg

Vlak

2008

Journal of General Virology

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The genus Nucleopolyhedrovirus (NPV) of the family Baculoviridae can be subdivided phylogenetically into two groups. The same division can be made on the basis of their budded virus (BV) envelope fusion protein. Group I NPVs are characterized by the presence of a GP64-like major envelope fusion protein, which is involved in viral attachment and the fusion of virus and cell membrane, and is required for budding of progeny nucleocapsids. Group II NPVs have an envelope fusion protein unrelated to GP64, named F. In contrast to GP64, F proteins are found in all baculoviruses, but they are not functional as envelope fusion proteins in group I NPVs. Autographa californica multiple NPV (AcMNPV) lacking GP64 can be pseudotyped by the F protein of Spodoptera exigua multiple NPV (SeMNPV), suggesting that F proteins are functionally analogous to GP64. GP64 homologues are thought to have been acquired by group I NPVs during evolution, thereby giving these viruses a selective advantage and obviating the need for a functional F protein. To address this supposition experimentally, attempts were made to pseudotype a group II NPV, SeMNPV, with GP64. Transfection of an f-null SeMNPV bacmid into Se301 cells did not result in the production of infectious BVs. This defect was rescued by insertion of SeMNPV f, but not by insertion of AcMNPV gp64. This suggests that the functional analogy between GP64 and F is not readily reciprocal and that F proteins from group II NPVs may provide additional functions in BV formation that are lacking in the GP64 type of fusion protein.

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“…4). HIV wild-type particles accumulated in gradient fractions at a density between 1n15 and 1n20 g\cm$ according to published sedimentation values (Shioda & Shibuta, 1990 ;Wagner et al, 1992) and displayed the typical processing pattern of Pr55 gag into p24\25 and the intermediate products p41\42. The same characteristics were observed for the mutants p24-TL and p24-CQG, indicating a rather wild-typelike appearance.…”

Section: Particle Formation and Production Of Infectious Hivmentioning

confidence: 99%

Inhibition of human immunodeficiency virus type 1 particle formation by alterations of defined amino acids within the C terminus of the capsid protein.

Kattenbeck

Poblotzki

Rohrhofer

et al. 1997

Journal of General Virology

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In previous studies, we demonstrated that the substitution of amino acid triplets for alanines in the carboxy-terminal portion (amino acids 341-352 : ATL EEM MTA CQC) of the capsid protein domain (p24) of human immunodeficiency virus type 1 (HIV-1) partly led to an inhibitory effect on the capacity to form virus-like particles (VLPs). In these experiments, the uncleaved Pr55 gag precursor protein was expressed by recombinant vaccinia viruses. We have now investigated the effects of these mutations with respect to a replication-competent HI-provirus system. Substitution of amino acids 344-346 (EEM) for alanines, which was previously shown to lead to

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Production of human immunodeficiency virus (HIV)-like particles from cells infected with recombinant vaccinia viruses carrying the gag gene of HIV

Cited by 122 publications

References 39 publications

Immune Response of Mice Infected with Recombinant Vaccinia Viruses Carrying the HIV gag Gene

Immune Response of Mice Infected with Recombinant Vaccinia Viruses Carrying the HIV gag Gene

GP64 of group I nucleopolyhedroviruses cannot readily rescue infectivity of group II f-null nucleopolyhedroviruses

Inhibition of human immunodeficiency virus type 1 particle formation by alterations of defined amino acids within the C terminus of the capsid protein.

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