ArticleJournal of virology1989
Expression of Sindbis virus 26S cDNA in Spodoptera frugiperda (Sf9) cells, using a baculovirus expression vector.
Article in Journal of virology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 19 citations in OpenAlex.
- Effective chikungunya virus-like particle vaccine produced in insect cells.PLoS neglected tropical diseases · 2013Article
- Factors affecting recombinant Western equine encephalitis virus glycoprotein production in the baculovirus system.Protein expression and purification · 2011Article
- Functional processing and secretion of Chikungunya virus E1 and E2 glycoproteins in insect cells.Virology journal · 2011Article
- Low temperature-dependent salmonid alphavirus glycoprotein processing and recombinant virus-like particle formation.PloS one · 2011Article
- The 3' end of Norwalk virus mRNA contains determinants that regulate the expression and stability of the viral capsid protein VP1: a novel function for the VP2 protein.Journal of virology · 2003Article
- Structural requirements for the assembly of Norwalk virus-like particles.Journal of virology · 2002Article
- Semliki Forest virus capsid protein expressed by a baculovirus recombinant.Archives of virology · 1993Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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 E1 protein, of 56 kDa) was inserted into the genome of Autographa 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 E1), 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-beta-N-acetylglucosaminidase H (endo-H) treatment of the recombinant glycoproteins, and by N-terminal sequence analysis of the E1 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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