Phosphorylation and Proteolytic Cleavage of Gag Proteins in Budded Simian Immunodeficiency Virus

Rue, Sarah; Roos, Jason W.; Tarwater, Patrick M.; Clements, Janice E.; Barber, Sheila A.

doi:10.1128/jvi.79.4.2484-2492.2005

Cited by 9 publications

(7 citation statements)

References 53 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…If we presume that the HIV IRES-driven Pr55 Gag isoforms function similarly to SIV p43 to suppress intracellular cleavage of Pr55 Gag , the difference in replication kinetics may be reconciled simply by comparing the processing of Pr55 Gag in budded HIV-1 and SIV virions. In this study and an earlier report, we demonstrate that processing of SIV Pr55 Gag can occur over time in budded virions (Rue et al, 2005). However, in HIV-1 it is not clear whether intravirion processing of Pr55 Gag occurs; one study suggested that processing of Pr55 Gag occurred either before the virion was released from the cell, or very shortly after budding (Kaplan, Manchester, and Swanstrom, 1994).…”

Section: Discussionsupporting

confidence: 54%

“…Proteolytic processing of Pr55 Gag in budded virions was carried out as previously described (Rue et al, 2005). Briefly, 293T cells were transfected as described above with proviral DNA for either WT SIVmac239 or SIVmac239 p43(-) and labeled with [ 35 S]Met/Cys as described above, except for only 1 h. Virus-containing supernatants were filtered, aliquoted, and incubated at 37ºC for different periods of time.…”

Section: Analysis Of Proteolytic Processing Of Pr55 Gag In Budded Virmentioning

confidence: 99%

“…To further examine the increase in maturation of SIVmac239 p43(-) virions, we used an assay previously described by our laboratory to examine processing of Pr55 Gag in budded WT SIVmac239 and SIVmac239 p43(-) virions over time (Rue et al, 2005). Briefly, 293T cells transfected with WT SIVmac239 or SIVmac239 p43(-) were labeled with [ 35 S]Met/Cys and virus-containing supernatants were aliquoted and incubated at 37ºC for different periods of time.…”

Section: Pr55 Gag Processing In Sivmac239 P43(-) Virionsmentioning

confidence: 99%

“…Late in the HIV/SIV lifecycle, Pr55 Gag and Pr160 Gag-Pol polyproteins oligomerize in the cytoplasm (Cen et al, 2004;Chiu, Yao, and Wang, 2002;Huang and Martin, 1997;Park and Morrow, 1992) and are targeted to the plasma membrane of the host cell (Bryant and Ratner, 1990;Gonzalez et al, 1993;Henderson et al, 1988;Yuan et al, 1993) where they initiate budding of the virion. During and after virion budding, the polyproteins are cleaved by the viral protease (PR) into their constitutive domains in a process referred to as maturation (Henderson et al, 1990;Kaplan, Manchester, and Swanstrom, 1994;Rue et al, 2005;Vogt, 1996). Maturation of virions begins when PR, initially present as a domain within Pr160 Gag-Pol , cleaves itself from the polyprotein (Debouck et al, 1987;Meek et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

The SIVmac239 Pr55Gag isoform, SIV p43, suppresses proteolytic cleavage of Pr55Gag

2007

Self Cite

View full text Add to dashboard Cite

In human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV) the gag gene encodes the precursor polyprotein Pr55Gag, which is cleaved by the viral protease to produce the major structural proteins. Recently, it has been shown that HIV and SIV gag RNAs contain internal ribosome entry sites (IRESs) that mediate translation of Pr55Gag [Pr57Gag in HIV type 2 (HIV-2)] isoforms. Previously, we demonstrated that SIVmac239 p43(-), a mutant that does not express the Pr55Gag isoform, SIV p43, replicates more efficiently than wild-type (WT) SIVmac239 in cell culture. In this study, we characterize SIVmac239 p43(-) virion production and demonstrate that, in the absence of SIV p43, cleavage of Pr55Gag is increased in budded virions, resulting in a higher percentage of mature particles. Additionally, intracellular cleavage of Pr55Gag is increased in SIVmac239 p43(-), suggesting that SIV p43 suppresses premature cleavage of Pr55Gag by the viral protease.

show abstract

Section: Discussionsupporting

confidence: 54%

Section: Analysis Of Proteolytic Processing Of Pr55 Gag In Budded Virmentioning

confidence: 99%

Section: Pr55 Gag Processing In Sivmac239 P43(-) Virionsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

The SIVmac239 Pr55Gag isoform, SIV p43, suppresses proteolytic cleavage of Pr55Gag

2007

Self Cite

View full text Add to dashboard Cite

show abstract

“…Whether it might be taking part in the cleavage of the VP7 still need further investigation. Approximately 5% of gag gene (such as lentiviruses, human immunodeficiency virus, simian immunodeficiency virus) produced other proteins causing by the ribosomal frameshift with independent functions (Rue, Roos, Tarwater, Clements, & Barber, 2005). Two mechanisms for generating more than one protein from a single mRNA have been reported.…”

Section: Tablementioning

confidence: 99%

Identification and characterization of vp7 gene in Bombyx mori cytoplasmic polyhedrosis virus

Zhu

et al. 2017

Gene

View full text Add to dashboard Cite

The genome of Bombyx mori cytoplasmic polyhedrosis virus (BmCPV) contains 10 double stranded RNA segments (S1-S10). The segment 7 (S7) encodes 50kDa protein which is considered as a structural protein. The expression pattern and function of p50 in the virus life cycle are still unclear. In this study, the viral structural protein 7 (VP7) polyclonal antibody was prepared with immunized mouse to explore the presence of small VP7 gene-encoded proteins in Bombyx mori cytoplasmic polyhedrosis virus. The expression pattern of vp7 gene was investigated by its overexpression in BmN cells. In addition to VP7, supplementary band was identified with western blotting technique. The virion, BmCPV infected cells and midguts were also examined using western blotting technique. 4, 2 and 5 bands were detected in the corresponding samples, respectively. The replication of BmCPV genome in the cultured cells and midgut of silkworm was decreased by reducing the expression level of vp7 gene using RNA interference. In immunoprecipitation experiments, using a polyclonal antiserum directed against the VP7, one additional shorter band in BmCPV infected midguts was detected, and then the band was analyzed with mass spectrum (MS), the MS results showed thatone candidate interacted protein (VP7 voltage-dependent anion-selective channel-like isoform, VDAC) was identified from silkworm. We concluded that the novel viral product was generated with a leaky scanning mechanism and the VDAC may be an interacted protein with VP7.

show abstract

Conserved serines in simian immunodeficiency virus capsid are required for virus budding

et al. 2005

View full text Add to dashboard Cite

The simian immunodeficiency virus (SIV) capsid protein (CA), a constituent of the Pr55Gag polyprotein, is phosphorylated in virions but not in virus-producing cells (Rue, S.M., Roos, J.W., Tarwater, P.M., Clements, J.E., Barber, S.A., 2005. Phosphorylation and proteolytic cleavage of gag proteins in budded simian immunodeficiency virus. J. Virol. 79 (4), 2484-2492.). Using phosphoamino acid analysis of CA, we show that serine is the primary phosphate acceptor. A series of substitution mutants of serines in the CA domain of Pr55Gag were constructed in the infectious viral clone SIVmac239. These virus mutants were examined for defects in virus replication and virion infectivity, release, and morphology, as well as alterations in phosphorylation of CA-containing proteins. Although the virus mutants exhibited a number of replication defects, none of these defects could be directly attributed to aberrant CA phosphorylation. A novel defect was a block in early budding, which was common among several virus mutants with substitutions in the CA N terminus. Together, these results indicate that certain residues in the CA N terminus are crucial for early budding events.

show abstract

Phosphorylation and Proteolytic Cleavage of Gag Proteins in Budded Simian Immunodeficiency Virus

Abstract: Gag and several of its cleavage intermediates likely precedes the cleavage of these domains by the viral protease.

Cited by 9 publications

References 53 publications

The SIVmac239 Pr55Gag isoform, SIV p43, suppresses proteolytic cleavage of Pr55Gag

The SIVmac239 Pr55Gag isoform, SIV p43, suppresses proteolytic cleavage of Pr55Gag

Identification and characterization of vp7 gene in Bombyx mori cytoplasmic polyhedrosis virus

Conserved serines in simian immunodeficiency virus capsid are required for virus budding

Contact Info

Product

Resources

About