Expression of the structural proteins of dengue 2 virus and yellow fever virus by recombinant vaccinia viruses

Hahn, Young S.; Lenches, Edith M.; Galler, Ricardo; Rice, Charles M.; Dalrymple, Joel M.; Strauss, James H.

doi:10.1007/bf01310534

Cited by 20 publications

(2 citation statements)

References 49 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This indicated a requirement for membrane translocation and the involvement of signal peptidases in protein processing. Regions encoding the viral nonstructural proteins were unnecessary for cleavage of structural proteins expressed either in vitro [21,27], or by recombinant vaccinia viruses [6,11,15,39].…”

Section: Introductionmentioning

confidence: 99%

Processing of dengue virus type 2 structural proteins containing deletions in hydrophobic domains

Gruenberg

Wright

1992

Archives of Virology

View full text Add to dashboard Cite

The 5' end of the genome of the dengue virus type 2 encoding the structural proteins was expressed using recombinant vaccinia virus. Three additional recombinants derived by deletion of selected dengue sequences within the parental construct were also expressed. They were designed to assess the role of hydrophobic domains in the processing of the viral polyprotein in intact cells. The first construct contained a deletion of nucleotides encoding most of the C protein; nucleotides encoding the hydrophobic domain at the carboxy terminus were retained. The second and third constructs contained smaller deletions of 72 bp and 129 bp encoding hydrophobic domains at the carboxy termini of C and prM respectively. Indirect immunofluorescence and radioimmunoprecipitation were used to detect prM and E in cells infected with recombinant viruses. The results showed that deletion of 90% of C had no apparent effect on the processing of prM and E, and that the signal sequence for E at the carboxy terminus of prM was active in the absence of the upstream signal sequence for prM at the carboxy terminus of C. Deletion of the hydrophobic sequences preceding the amino terminus of E prevented cleavage at the prM-E junction. These results obtained using infected cells were consistent with the published findings for the translation of flavivirus RNA in vitro, and indicated the importance of membrane association in the cleavage of structural proteins from the flavivirus polyprotein. In addition, cells infected with the recombinant virus containing the large deletion in the C coding region released the E glycoprotein into the culture medium.

show abstract

Section: Introductionmentioning

confidence: 99%

Processing of dengue virus type 2 structural proteins containing deletions in hydrophobic domains

Gruenberg

Wright

1992

Archives of Virology

View full text Add to dashboard Cite

show abstract

“…The Autographacalifornicanuclearpolyhedrosisvirus (AcNPV) D2 EA 102 gene was recombined into the AcRp231acZ genome as described previously [4] Several strategies have been explored to produce this antigen in a form that conserves its protective efficacy as evaluated in animal models. DEN E-glycoproteins, produced either in vaccinia or in baculovirus vectors show variations in processing, antigenicity and immunogenic properties [3,4,5,6,11,19,20,26,27]. It is unclear whether the low immunogenicity of some of these E-protein constructs is related to the virus vector, to the DEN serotype or to the nature of the construct.…”

mentioning

confidence: 99%

Protective efficacy in mice of a secreted form of recombinant dengue-2 virus envelope protein produced in baculovirus infected insect cells

Delenda

Frenkiel

Denis

1994

Archives of Virology

View full text Add to dashboard Cite

We constructed a recombinant baculovirus encoding a dengue (DEN)-2 virus envelope glycoprotein truncated of 102 amino acids (aa) at its C-terminus (D2E delta 102). The production, processing and transportation of the recombinant protein in baculovirus-infected Spodoptera frugiperda (Sf9) cells and its immunogenic properties in mice were compared to those of a previously characterized recombinant DEN-2 E-protein with a 71aa C-terminal truncation (D2E delta 71). Both proteins were transported through the Golgi complex and their N-oligosaccharides of the high mannose type were processed to the complex mannose type. D2E delta 102 transited to the plasma membrane and was secreted whereas D2E delta 71 presumably remained associated with the plasma membrane. The reactivities of the recombinant proteins with neutralizing monoclonal antibodies were similar. Both intracellular and extracellular D2E delta 102 induced neutralizing antibodies in mice and were thus immunogenic. The level of protective immunity to DEN-2 virus encephalitis challenge in mice vaccinated with intracellular D2E delta 102 (80%, p < 0.01) was lower than that induced with D2E delta 71 (90%, P < 0.001). Sixty-eight percent (P < 0.001) of mice vaccinated with 5 micrograms of extracellular D2E delta 102 protein were protected against lethal challenge.

show abstract

Poxviruses as Genetic Vectors

Cox¹,

Gettig²,

Paoletti³

1995

Viruses in Human Gene Therapy

View full text Add to dashboard Cite

Expression of the structural proteins of dengue 2 virus and yellow fever virus by recombinant vaccinia viruses

Cited by 20 publications

References 49 publications

Processing of dengue virus type 2 structural proteins containing deletions in hydrophobic domains

Processing of dengue virus type 2 structural proteins containing deletions in hydrophobic domains

Protective efficacy in mice of a secreted form of recombinant dengue-2 virus envelope protein produced in baculovirus infected insect cells

Poxviruses as Genetic Vectors

Contact Info

Product

Resources

About