Further Analysis of The Effect of Ca2+ on Morphogenesis of HVJ (Sendai Virus) in LLC-MK2 Cells: Effects on Phosphorylated M Protein Associated with Viral Morphogenesis.

Kim, Jeman

doi:10.1247/csf.19.325

Cited by 5 publications

(7 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We have been studying the mechanism of membrane fusion, using experimental systems of enveloped virus infection [1][2][3] and myoblast differentiation [4][5][6]. In the life cycle of an enveloped virus, both viral penetration and budding are associated with membrane fusion.…”

Section: Introductionmentioning

confidence: 99%

Temperature-Sensitive Viral Infection: Inhibition of Hemagglutinating Virus of Japan (Sendai Virus) Infection at 41°

et al. 2002

Self Cite

View full text Add to dashboard Cite

While investigating myoblast fusion using enveloped viruses, we unexpectedly found that the production of hemagglutinating virus of Japan (HVJ; Sendai virus) was suppressed temperature dependently in quail myoblasts transformed with a temperature-sensitive Rous sarcoma virus, which proliferate at 35.5° but differentiate at 41°; viral production was normal at 35.5° but suppressed at 41° irrespective of the species of host cells. The production of some viruses, i.e. measles virus, influenza virus, herpes simplex virus type 1 and poliovirus, was also markedly suppressed at 41°, suggesting that a temperature of 41° affects viral infection generally. To clarify the mechanism of the suppression, the infectious pattern of HVJ was examined both at 37° and at 41° in LLC-MK2 cells. The synthesis of HVJ-specific proteins was inhibited at the transcriptional level at 41°, although viral penetration by envelope fusion was not affected. The transcriptional inhibition was also seen in quail fibroblasts, which do not express a 70-kD heat shock protein (HSP70), suggesting that HSP70 is dispensable for the inhibition of viral gene transcription at 41°. Further, when the infected cells were incubated at 41° after the viral proteins had been synthesized at 37°, viral production was also inhibited. Immunofluorescent staining of the cells exposed to 41° showed that HVJ envelope proteins formed large aggregates on the cell surface, into which both M and NP proteins were assembled. Under the electron microscope, HVJ virions appeared normal even at 41°, but were detected in clusters on the cell surface, unlike at 37°. These observations suggested that the release of HVJ virions from the cell surface was inhibited for some reason at 41°. Consequently, it was indicated that two steps, viral gene transcription and the release of virions, were inhibited at 41°.

show abstract

Section: Introductionmentioning

confidence: 99%

Temperature-Sensitive Viral Infection: Inhibition of Hemagglutinating Virus of Japan (Sendai Virus) Infection at 41°

et al. 2002

Self Cite

View full text Add to dashboard Cite

show abstract

“…5A-c, B-c). The patch-like distribution of viral proteins was previously suggested to correspond to collective budding sites of viral virions [4,8]. Also, in the cells at 41°, F protein was similarly observed, although the patches seemed to decrease as compared to cells at 37° ( fig.…”

mentioning

confidence: 51%

“…In the propagation of HVJ, viral-specific proteins synthesized in cytoplasm are transported to the cell membrane and assembled there into progeny virions [5,7,8] …”

Section: Exposure Of Hn Protein On the Cell Surface Is Prevented At 41°tmentioning

confidence: 99%

“…In the morphogenesis of HVJ, it is known that envelope proteins interact with M protein and NP of the nucleocapsid at the budding sites for assembly [4,[6][7][8]. Finally, it was examined whether such an assembly of viral proteins occurred at 41° even if HN protein was not integrated into the cell membrane.…”

Section: Assembly Of M Protein and Np At 41°omentioning

confidence: 99%

“…Viral envelope proteins (HN and F proteins) synthesized on membrane-bound ribosomes are transported through an exocytic pathway, integrated into the cell membrane and form spike structures [1,4,5]. Envelope proteins interact with the NP of the nucleocapsid by the bridging of M protein [6][7][8]. After the assembly of viral components, the nucleocapsid is wrapped with the cell membrane, including envelope proteins, and finally, a progeny virion buds off from the cell membrane into the extracellular space [4,9].…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Characterization of Temperature-Sensitive HVJ (Sendai Virus) Infection in Vero Cells: Inhibitory Mechanism of Viral Production at 41°

Hirayama¹,

Ishida²,

Sugimoto³

et al. 2003

Intervirology

Self Cite

View full text Add to dashboard Cite

In a previous study, it was found that the synthesis of hemagglutinating virus of Japan (HVJ; Sendai virus)-specific proteins was inhibited at the transcriptional level at 41° in LLC-MK2 cells. During an investigation of the temperature sensitivity of HVJ production in other host cells, the synthesis of HVJ-specific proteins was recognized even at 41° in Vero cells. Viral production, however, was not detected, indicating the inhibition of steps after the synthesis of viral proteins. Hemadsorption activity was not detected at 41°, suggesting problems with the envelope proteins, especially hemagglutinin-neuraminidase (HN) protein, at the cell membrane. Immunofluorescent staining and surface immunoprecipitation showed that HN protein was not present on the surface in spite of its localization in the cytoplasm. Further, analysis of the cell membrane fraction suggested that fusion (F) protein was integrated into the cell membrane but HN protein was not at 41°. Electron microscopic observation showed that budding sites with spike structures formed and nucleocapsids assembled under the sites at 41° without HN protein, although budded HVJ virions were not detected. At this time, F protein was exposed to the cell membrane and interacted with matrix and nucleocapsid proteins. The results suggested that the suppression of HVJ production at 41° was due to the absence of HN protein in the membrane of Vero cells.

show abstract

Budding of enveloped viruses from the plasma membrane

1997

View full text Add to dashboard Cite

Many enveloped viruses are released from infected cells by maturing and budding at the plasma membrane. During this process, viral core components are incorporated into membrane vesicles that contain viral transmembrane proteins, termed 'spike' proteins. For many years these spike proteins, which are required for infectivity, were believed to be incorporated into virions via a direct interaction between their cytoplasmic domains and viral core components. More recent evidence shows that, while such direct interactions drive budding of alphaviruses, this may not be the case for negative strand RNA viruses and retroviruses. These viruses can bud particles in the absence of spike proteins, using only viral core components to drive the process. In some cases the spike proteins, without the viral core, can be released as virus-like particles. Optimal budding and release may, therefore, depend on a 'push-and-pull' concerted action of core and spike, where oligomerization of both components plays a crucial role.

show abstract

Further Analysis of The Effect of Ca2+ on Morphogenesis of HVJ (Sendai Virus) in LLC-MK2 Cells: Effects on Phosphorylated M Protein Associated with Viral Morphogenesis.

Cited by 5 publications

References 27 publications

Temperature-Sensitive Viral Infection: Inhibition of Hemagglutinating Virus of Japan (Sendai Virus) Infection at 41°

Temperature-Sensitive Viral Infection: Inhibition of Hemagglutinating Virus of Japan (Sendai Virus) Infection at 41°

Characterization of Temperature-Sensitive HVJ (Sendai Virus) Infection in Vero Cells: Inhibitory Mechanism of Viral Production at 41°

Budding of enveloped viruses from the plasma membrane

Contact Info

Product

Resources

About