Envelope proteins of Semliki Forest virus synthesized in Xenopus oocytes are transported to the cell surface.

Huth, Antje; Rapoport, Tom A.; Kääriäinen, Leevi

doi:10.1002/j.1460-2075.1984.tb01882.x

Cited by 14 publications

(4 citation statements)

References 47 publications

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“…The last cleavage in the processing of the alphavirus structural proteins, that of PE2 to E2 and E3 (20, 29,59), has been postulated to be catalyzed by a Golgi protease during transit to the plasma membrane (9, 37). The expression experiments reported here as well as other expression experiments using Semliki Forest virus (19) show that this processing can occur in the absence of virus budding.…”

Section: Isolation Of a Vaccinia Recombinant Containing Sindbissupporting

confidence: 67%

Expression of Sindbis virus structural proteins via recombinant vaccinia virus: synthesis, processing, and incorporation into mature Sindbis virions

Rice¹,

Franke²,

Strauss³

et al. 1985

J Virol

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We have obtained a vaccinia virus recombinant which contains a complete cDNA copy of the 26S RNA of Sindbis virus within the thymidine kinase gene of the vaccinia virus genome. This recombinant constitutively transcribed the Sindbis sequences throughout the infectious cycle, reflecting the dual early-late vaccinia promoter used in this construction. The Sindbis-derived transcripts were translationally active, giving rise to both precursor and mature structural proteins of Sindbis virus, including the capsid protein (C), the precursor of glycoprotein E2 (PE2), and the two mature envelope glycoproteins (El and E2). These are the same products translated from the 26S mRNA during Sindbis infection, and thus these proteins were apparently cleaved, glycosylated, and transported in a manner analogous to that seen during authentic Sindbis infections. By using epitope-specific antibodies, it was possible to demonstrate that recombinant-derived proteins were incorporated into Sindbis virions during coinfections with monoclonal antibody-resistant Sindbis variants. These results suggest that all the information necessary to specify the proper biogenesis of Sindbis virus structural proteins resides within the 26S sequences and that vaccinia may provide an appropriate system for using DNA molecular genetic manipulations to unravel a variety of questions pertinent to RNA virus replication.

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Section: Isolation Of a Vaccinia Recombinant Containing Sindbissupporting

confidence: 67%

Expression of Sindbis virus structural proteins via recombinant vaccinia virus: synthesis, processing, and incorporation into mature Sindbis virions

Rice¹,

Franke²,

Strauss³

et al. 1985

J Virol

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show abstract

“…Efficient transport of alphavirus glycoproteins beyond the ER normally requires dimerization (and possibly higher-order oligomerization) of the glycoproteins but does not require expression of capsid protein or of nonstructural proteins (140,220,264,265,309,417,423,432,603). Monomeric E2 of SF was transported inefficiently but detectably to the cell surface, whereas monomeric El was not detectably transported beyond the ER.…”

Section: Pe2mentioning

confidence: 99%

The alphaviruses: gene expression, replication, and evolution.

Strauss¹,

Strauss²

1994

Microbiological Reviews

1,390

1,135

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“…The replication strategy of Sindbis virus in vertebrate cells has been very comprehensively studied (3, 8, 26-28, 32, 33). Correct processing of this polyprotein can occur in the absence of viral genomic RNA, suggesting that the nonstructural proteins of the virus are not involved or necessary for the processing of the structural proteins (14,23). Thus, expression of the subgenomic mRNA of Sindbis virus was considered a good model with which to study protein processing in this insect cell line with the baculovirus as a vector.…”

Section: Discussionmentioning

confidence: 99%

Expression of Sindbis virus 26S cDNA in Spodoptera frugiperda (Sf9) cells, using a baculovirus expression vector

Oker‐Blom

Summers

1989

J Virol

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To study protein processing in an insect Spodoptera frugiperda (fall armyworm; Sf9) cell line, a 26S cDNA encoding the sequence of Sindbis virus structural proteins (capsid protein, of 30 kilodaltons [kDa]; p62 [the precursor of E3 and E2], of 62 kDa; a 6-kDa peptide; and the El protein, of 56 kDa) was inserted into the genome ofAutographa californica nuclear polyhedrosis virus (AcNPV) adjacent to the polyhedrin promoter. By immunoblot analysis with antisera directed against whole Sindbis virus and the individual structural proteins (capsid, E2, and El), we have shown that polypeptides similar in size and antigenicity to those synthesized in Sindbis virus-infected BHK cells are expressed in Sf9 cells infected with the recombinant baculovirus Ac373-SV26. By pulse-chase labeling in the presence or absence of tunicamycin, by endo-P-N-acetylglucosaminidase H (endo-H) treatment of the recombinant glycoproteins, and by N-terminal sequence analysis of the El envelope glycoprotein, we have further shown that the 26S transcription translation unit of Sindbis virus, although normally encoded by nonnuclear RNA, is expressed and proteolytically cleaved similarly, if not identically, in Sf9 cells as compared with BHK cells when a baculovirus expression vector is used.

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Envelope proteins of Semliki Forest virus synthesized in Xenopus oocytes are transported to the cell surface.

Cited by 14 publications

References 47 publications

Expression of Sindbis virus structural proteins via recombinant vaccinia virus: synthesis, processing, and incorporation into mature Sindbis virions

Expression of Sindbis virus structural proteins via recombinant vaccinia virus: synthesis, processing, and incorporation into mature Sindbis virions

The alphaviruses: gene expression, replication, and evolution.

Expression of Sindbis virus 26S cDNA in Spodoptera frugiperda (Sf9) cells, using a baculovirus expression vector

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