Location, transcription, and sequence of a baculovirus gene encoding a small arginine-rich polypeptide

Wilson, Marijo E.; Mainprize, T H; Friesen, Paul D.; Miller, Lois K.

doi:10.1128/jvi.61.3.661-666.1987

Cited by 129 publications

(32 citation statements)

References 36 publications

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“…It is has been suggested that the positively charged arginine residues of Basic Protein interact with the negatively charged DNA backbone to enable its condensation in the nucleocapsid (Kelly et al, 1983). Basic Protein is protamine-like (Tweeten et al, 1980) and has been called P6.9 or VP12 depending on the baculovirus (Wilson and Price, 1988;Wilson et al, 1987). Basic Protein is also a phosphoprotein and its phosphorylation is inhibited by the presence of Zn 2þ Consigli, 1992, 1993;Wilson and Consigli, 1985).…”

Section: B Nucleoprotein Corementioning

confidence: 99%

The Baculoviruses Occlusion‐Derived Virus: Virion Structure and Function

Slack

Arif

2006

Advances in Virus Research

264

240

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Section: B Nucleoprotein Corementioning

confidence: 99%

The Baculoviruses Occlusion‐Derived Virus: Virion Structure and Function

Slack

Arif

2006

Advances in Virus Research

264

240

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“…In this study, we determined whether the 18 lefs are required for expression from two other promoters representative of the late and very late classes of transcription and whether vlf-1 exerted a specific effect on the very late class of promoters in transient-expression assays. The late p6.9 promoter drives expression of a basic 6.9-kDa protamine-like protein (P6.9) which is associated with viral DNA within the nucleocapsid, forming the nucleoprotein core of virus particles (53,58). Very late p10 encodes an abundant protein of 10 kDa which forms large fibrillar structures in both the cytoplasm and nucleus of infected cells during the very late phase of infection (55,57).…”

mentioning

confidence: 99%

Factors regulating baculovirus late and very late gene expression in transient-expression assays

Todd

Passarelli

et al. 1996

J Virol

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Eighteen genes of Autographa californica nuclear polyhedrosis virus are necessary and sufficient to transactivate expression from the late vp39 promoter in transient-expression assays in SF-21 cells. These 18 genes, known as late expression factor genes (lefs), are also required to transactivate the very late promoter of the polyhedrin gene, polh, but expression from this promoter is relatively weak compared with expression from the vp39 promoter. To further define the factors required for late and very late promoter expression, we first determined that the eighteen lefs were also required for expression from two other major baculovirus promoters: the late basic 6.9-kDa protein gene, p6.9, and the very late 10-kDa protein gene, p10. We next examined the effect of the very late expression factor 1 gene (vlf-1), a gene previously identified by analysis of a temperaturesensitive mutant, in the transient-expression assay and found that vlf-1 specifically transactivated the two very late promoters but not the two late promoters. We then surveyed the Autographa californica nuclear polyhedrosis virus genome for additional genes which might specifically regulate very late gene expression; no additional vlf genes were detected, suggesting that VLF-1 is the primary regulator of very late gene expression. Finally, we found that the relative contribution of the antiapoptosis gene p35, which behaves as a lef in these transient-expression assays, depended on the nature of the other viral genes provided in the cotransfection mixtures, suggesting that other viral genes also contribute to the ability of the virus to block apoptosis.

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“…Also, proteins with regulatory and/or enzyme activity functions were found. However, an essential 78-kDa phosphoprotein and a 6.9-kDa major core protein with a small arginine-rich polypeptide were not found, which are known to be important for the formation of nucleoprotein complex of baculovirions 32,33 . Nonetheless, these results indicate that there are some baculovirus-derived proteins in the preparation of purified H5 VLPs.…”

Section: Identification Of Baculovirus Vector Derived Proteinsmentioning

confidence: 97%

Proteomic Characterization of Influenza H5N1 Virus-like Particles and Their Protective Immunogenicity

et al. 2011

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Recombinant virus-like particles (VLPs) have been shown to induce protective immunity. Despite of their potential significance as promising vaccine candidates, the protein composition of VLPs produced in insect cells has not been well characterized. Here we report a proteomic analysis of influenza VLPs containing hemagglutinin (HA) and matrix M1 proteins from a human isolate of avian influenza H5N1 virus (H5 VLPs) produced in insect cells using the recombinant baculovirus expression system. Comprehensive proteomic analysis of purified H5 VLPs identified viral proteins and 37 additional host-derived proteins, many of which are known to be present in other enveloped viruses. Proteins involved in different cellular structures and functions were found to be present in H5 VLPs including those from the cytoskeleton, translation, chaperone, and metabolism. Immunization with purified H5 VLPs induced protective immunity, which was comparable to the inactivated whole virus containing all viral components. Unpurified H5 VLPs containing excess amounts of non-influenza soluble proteins also conferred 100% protection against lethal challenge although lower immune responses were induced. These results provide important implications consistent with the idea that VLP production in insect cells may involve similar cellular machinery as other RNA enveloped viruses during synthesis, assembly, trafficking, and budding processes.

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Location, transcription, and sequence of a baculovirus gene encoding a small arginine-rich polypeptide

Cited by 129 publications

References 36 publications

The Baculoviruses Occlusion‐Derived Virus: Virion Structure and Function

The Baculoviruses Occlusion‐Derived Virus: Virion Structure and Function

Factors regulating baculovirus late and very late gene expression in transient-expression assays

Proteomic Characterization of Influenza H5N1 Virus-like Particles and Their Protective Immunogenicity

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