Uukuniemi virus glycoproteins accumulate in and cause morphological changes of the Golgi complex in the absence of virus maturation

Gahmberg, Nina; Kuismanen, Esa; Keränen, Sirkka; Pettersson, Ralf F.

doi:10.1128/jvi.57.3.899-906.1986

Cited by 44 publications

(25 citation statements)

References 41 publications

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“…The envelope proteins of these viruses are synthesized in the ER using the same machinery as host membrane proteins, and they are then targeted to the assembly compartment prior to budding. Once budded into the lumen of the ER or Golgi, the particles range from 70 to 160 nm, and dilation and even disassembly of the Golgi have been observed during infection (Ulasli et al 2010;Gahmberg et al 1986;Lavi et al 1996). The advantage(s) of intracellular assembly are unknown.…”

Section: Enveloped Viruses That Assemble At Intracellular Membranesmentioning

confidence: 99%

“…Bunyaviruses and rubella virus have not been reported to encode ion channels. However, the Golgi complex is disrupted in cells infected with the Uukuniemi bunyavirus (Gahmberg et al 1986). The disrupted Golgi can still transport and process cargo (Gahmberg et al 1986), similar to the coronavirus findings.…”

Section: Release Of Other Enveloped Viruses That Assemble Intracellulmentioning

confidence: 99%

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Accommodation of large cargo within Golgi cisternae

Machamer

2013

Histochem Cell Biol

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In mammalian cells, the Golgi complex has an elaborate structure consisting of stacked, flattened cisternal membranes collected into a ribbon in the center of the cell. Amazingly, the flattened cisternae can rapidly dilate to accommodate large cargo as it traffics through the organelle. The mechanism by which this occurs is unknown. Exocytosis of large cargo is essential for many physiological processes, including collagen and lipoprotein secretion, and defects in the process lead to disease. In addition, enveloped viruses that bud into the endoplasmic reticulum or Golgi complex must also be transported through Golgi cisternae for secretion from the infected cell. This review summarizes our understanding of intra-Golgi transport of large cargo, and outlines current questions open for experimentation.

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Section: Enveloped Viruses That Assemble At Intracellular Membranesmentioning

confidence: 99%

Section: Release Of Other Enveloped Viruses That Assemble Intracellulmentioning

confidence: 99%

Accommodation of large cargo within Golgi cisternae

Machamer

2013

Histochem Cell Biol

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“…The glycoproteins of bunyaviruses are model Golgi membrane proteins, since the viruses are formed by budding at the smooth membranes of the Golgi complex (Murphy et a/., 1973;Smith and Pifat, 1982) and the viral glycoproteins accumulate in the Golgi complex during virus infection (Chen et al, 1991;Gahmberg et a/., 1986;Kuismanen et a/., 1982Kuismanen et a/., , 1984Madoff and Lenard, 1982) as well as when expressed by recombinant vaccinia viruses (Matsuoka et al, 1988;Pensiero et a/., 1988;Pettersson et al,, 1988;Wasmoen et a/., 1988). Punta Toro virus (PTV) is a member of the phlebovirus genus of the family Bunyaviridae (Bishop et al, 1980).…”

Section: Introductionmentioning

confidence: 99%

Golgi complex localization of the Punta Toro virus G2 protein requires its association with the G1 protein

1991

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The glycoproteins of bunyaviruses accumulate in membranes of the Golgi complex, where virus maturation occurs by budding. In this study we have constructed a series of full length or truncated mutants of the G2 glycoprotein of Punta Toro virus (PTV), a member of the Phlebovirus genus of the Bunyaviridae, and investigated their transport properties. The results indicate that the hydrophobic domain preceding the G2 glycoprotein can function as a translocational signal peptide, and that the hydrophobic domain near the C-terminus serves as a membrane anchor. A G2 glycoprotein construct with an extra hydrophobic sequence derived from the N-terminal NSM region was stably retained in the ER, and was unable to be transported to the Golgi complex. The full-length G2 glycoprotein, when expressed on its own, was transported out of the ER and expressed on the cell surface, whereas the G1 and G2 proteins when expressed together are retained in the Golgi complex. A truncated anchor-minus form of the G2 glycoprotein was found to be secreted into the culture medium, but was retained in the Golgi complex when coexpressed with the G1 glycoprotein. These results indicate that the G2 membrane glycoprotein is a class I membrane protein which does not contain a signal sufficient for Golgi retention, and suggest that its Golgi localization is a result of association with the G1 glycoprotein.

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“…By immunofluorescent microscopy, Kuismanen and colleagues showed that in cells infected with Uukuniemi virus the Golgi region underwent an expansion and became vacuolized . Both glycoproteins, Gl and G2, accumulated in the Golgi region during virus infection; neither polypeptide could be chased out of the Golgi even after a 6-hr treatment with cycloheximide (Gahmberg et al, 1986), conditions that would allow complete transport of the Semliki Forest virus membrane proteins from the Golgi (Green et al, 1981a). Furthermore, the glycoproteins of a temperature-sensitive strain of Uukuniemi virus were retained in the Golgi even under conditions where no virus maturation took place and no nucleocapsids accumulated in the Golgi region (Gahmberg et al, 1986).…”

Section: B Viral Polypeptides As Probes For Intracellular Compartmentsmentioning

confidence: 97%

Membrane Insertion and Transport of Viral Glycoproteins: A Mutational Analysis

Hunter¹

1988

Protein Transfer and Organelle Biogenesis

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Uukuniemi virus glycoproteins accumulate in and cause morphological changes of the Golgi complex in the absence of virus maturation

Cited by 44 publications

References 41 publications

Accommodation of large cargo within Golgi cisternae

Accommodation of large cargo within Golgi cisternae

Golgi complex localization of the Punta Toro virus G2 protein requires its association with the G1 protein

Membrane Insertion and Transport of Viral Glycoproteins: A Mutational Analysis

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