Rift valley fever virus M segment: Cellular localization of M segment-encoded proteins

Wasmoen, Terri; Kakach, L T; Collett, Marc S.

doi:10.1016/0042-6822(88)90174-2

Cited by 51 publications

(44 citation statements)

References 14 publications

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“…Earlier studies demonstrated that vaccinia virus-expressed RVFV genes, which either included or eliminated the preglycoprotein coding region, trafficked normally through the Golgi [33]. A more recent study, with a T7 expression system, confirmed these earlier results and further demonstrated that the Golgi localization signal is found in Gn in a region consisting of a 20 amino acid transmembrane domain and the adjacent 28 amino acids of the cytosolic tail [34].…”

Section: Discussionsupporting

confidence: 72%

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Immunogenicity of combination DNA vaccines for Rift Valley fever virus, tick-borne encephalitis virus, Hantaan virus, and Crimean Congo hemorrhagic fever virus

Spik

Shurtleff

McElroy

et al. 2006

Vaccine

131

109

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DNA vaccines for Rift Valley fever virus (RVFV), Crimean Congo hemorrhagic fever virus (CCHFV), tick-borne encephalitis virus (TBEV), and Hantaan virus (HTNV), were tested in mice alone or in various combinations. The bunyavirus vaccines (RVFV, CCHFV, and HTNV) expressed Gn and Gc genes, and the flavivirus vaccine (TBEV) expressed the preM and E genes. All vaccines were delivered by gene gun. The TBEV DNA vaccine and the RVFV DNA vaccine elicited similar levels of antibodies and protected mice from challenge when delivered alone or in combination with other DNAs. Although in general, the HTNV and CCHFV DNA vaccines were not very immunogenic in mice, there were no major differences in performance when given alone or in combination with the other vaccines. Published by Elsevier Ltd.

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Section: Discussionsupporting

confidence: 72%

“…The glycosylation site, which is used during translation from the first ATG, is not used in translation from the second ATG [32]. Although it is not clear if the fourth in-frame ATG is used by RVFV during infection, it can be used to generate Gn and Gc in a variety of expressions systems ( [21,[30][31][32][33], this report).…”

Section: Discussionmentioning

confidence: 99%

Immunogenicity of combination DNA vaccines for Rift Valley fever virus, tick-borne encephalitis virus, Hantaan virus, and Crimean Congo hemorrhagic fever virus

Spik

Shurtleff

McElroy

et al. 2006

Vaccine

131

109

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“…The envelope glycoproteins, G N and G C , of RVF virus have been found to localize to the Golgi apparatus both in RVF virus-infected cells and when expressed as a polyprotein from a vaccinia virus recombinant (31). To eliminate potential effects on the Golgi mediated by vaccinia virus, we utilized a T7 expression system in which BHK-T7 cells (that are stably transformed with a plasmid that expresses T7 polymerase) are transfected with the glycoprotein expression plasmids outlined in Fig.…”

Section: Aminomentioning

confidence: 99%

“…Localization of the envelope glycoproteins is a crucial step in the virus maturation process. The two RVF virus envelope glycoproteins localize to the Golgi apparatus in the absence of other virally encoded proteins (31), and thus one or both of these glycoproteins contains a Golgi localization signal. Following Golgi localization, the remaining structural proteins and the genome are recruited, followed by viral budding.…”

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confidence: 99%

Characterization of the Golgi Retention Motif of Rift Valley Fever Virus G _N Glycoprotein

Gerrard

Nichol

2002

J Virol

107

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As Rift Valley fever (RVF) virus, and probably all members of the family Bunyaviridae, matures in the Golgi apparatus, the targeting of the virus glycoproteins to the Golgi apparatus plays a pivotal role in the virus replication cycle. No consensus Golgi localization motif appears to be shared among the glycoproteins of these viruses. The viruses of the family Bunyaviridae synthesize their glycoproteins, GN and GC, as a polyprotein. The Golgi localization signal of RVF virus has been shown to reside within the GN protein by use of a plasmid-based transient expression system to synthesize individual GN and GC proteins. While the distribution of individually expressed GN significantly overlaps with cellular Golgi proteins such as β-COP and GS-28, GC expressed in the absence of GN localizes to the endoplasmic reticulum. Further analysis of expressed GN truncated proteins and green fluorescent protein/GN chimeric proteins demonstrated that the RVF virus Golgi localization signal mapped to a 48-amino-acid region of GN encompassing the 20-amino-acid transmembrane domain and the adjacent 28 amino acids of the cytosolic tail

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“…Like orthobunyaviruses, phleboviruses encode their NSm proteins as part of a precursor with the glycoproteins (9,18,56), whereas NSm of tospoviruses is translated from a subgenomic mRNA in an ambisense manner (21,27). Little is known about the function of NSm encoded by orthobunyaviruses or phleboviruses.…”

mentioning

confidence: 99%

Requirement of the N-Terminal Region of Orthobunyavirus Nonstructural Protein NSm for Virus Assembly and Morphogenesis

Shi

Kohl

Léonard

et al. 2006

J Virol

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The nonstructural protein NSm of Bunyamwera virus (BUNV), the prototype of the Bunyaviridae family, is encoded by the M segment in a polyprotein precursor, along with the virion glycoproteins, in the order Gn-NSm-Gc. As little is known of its function, we examined the intracellular localization, membrane integrality, and topology of NSm and its role in virus replication. We confirmed that NSm is an integral membrane protein and that it localizes in the Golgi complex, together with Gn and Gc. Coimmunoprecipitation assays and yeast two-hybrid analysis demonstrated that NSm was able to interact with other viral proteins. NSm is predicted to contain three hydrophobic (I, III, and V) and two nonhydrophobic (II and IV) domains. The N-terminal nonhydrophobic domain II was found in the lumen of an intracellular compartment. A novel BUNV assembly assay was developed to monitor the formation of infectious virus-like-particles (VLPs). Using this assay, we showed that deletions of either the complete NSm coding region or domains I, II, and V individually seriously compromised VLP production. Consistently, we were unable to rescue viable viruses by reverse genetics from cDNA constructs that contained the same deletions. However, we could generate mutant BUNV with deletions in NSm domains III and IV and also a recombinant virus with the green fluorescent protein open reading frame inserted into NSm domain IV. The mutant viruses displayed differences in their growth properties. Overall, our data showed that the N-terminal region of NSm, which includes domain I and part of domain II, is required for virus assembly and that the C-terminal hydrophobic domain V may function as an internal signal sequence for the Gc glycoprotein.

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Rift valley fever virus M segment: Cellular localization of M segment-encoded proteins

Cited by 51 publications

References 14 publications

Immunogenicity of combination DNA vaccines for Rift Valley fever virus, tick-borne encephalitis virus, Hantaan virus, and Crimean Congo hemorrhagic fever virus

Immunogenicity of combination DNA vaccines for Rift Valley fever virus, tick-borne encephalitis virus, Hantaan virus, and Crimean Congo hemorrhagic fever virus

Characterization of the Golgi Retention Motif of Rift Valley Fever Virus G _N Glycoprotein

Requirement of the N-Terminal Region of Orthobunyavirus Nonstructural Protein NSm for Virus Assembly and Morphogenesis

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Rift valley fever virus M segment: Cellular localization of M segment-encoded proteins

Cited by 51 publications

References 14 publications

Immunogenicity of combination DNA vaccines for Rift Valley fever virus, tick-borne encephalitis virus, Hantaan virus, and Crimean Congo hemorrhagic fever virus

Immunogenicity of combination DNA vaccines for Rift Valley fever virus, tick-borne encephalitis virus, Hantaan virus, and Crimean Congo hemorrhagic fever virus

Characterization of the Golgi Retention Motif of Rift Valley Fever Virus G N Glycoprotein

Requirement of the N-Terminal Region of Orthobunyavirus Nonstructural Protein NSm for Virus Assembly and Morphogenesis

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Characterization of the Golgi Retention Motif of Rift Valley Fever Virus G _N Glycoprotein