Literature DB >> 8920817

The fragmentation of incoming Semliki Forest virus nucleocapsids in mosquito (Aedes albopictus) cells might be coupled to virion uncoating.

B Mrkic1, C Kempf.   

Abstract

The fate of Semliki Forest virus (SFV) nucleocapsid, especially the capsid protein (C-protein), was investigated during the early stages of a productive infection in mosquito Aedes albopictus cells. Infection of the cells resulted in a time dependent accumulation of a C-protein derived fragment. This fragmentation of incoming viral nucleocapsid was prevented by NH4Cl, an agent generally used to elevate the pH in acidic intracellular compartments, suggesting that a low intravesicular pH is required for this process. Density gradient analysis of the postnuclear cell lysate demonstrated that the fragmentation was associated with a cellular compartment showing a density of 1.14 +/- 0.02 g/ml. This cellular compartment was devoid from a lysosomal marker enzyme and represented the timely preceding cellular fraction through which SFV passed before encountering a lysosomal fraction. Furthermore, the intracellular distribution of the viral, 3H-uridine-labeled RNA suggested that the same fraction might represent a key cellular compartment in which the separation of the viral RNA from the viral structural proteins is primed. In conclusion, these data lead to the suggestion that the fragmentation of incoming SFV nucleocapsids in Aedes albopictus cells might be the part of the mechanism leading to the release of viral RNA into the cytosol during early stages of productive infection.

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Year:  1996        PMID: 8920817     DOI: 10.1007/bf01718196

Source DB:  PubMed          Journal:  Arch Virol        ISSN: 0304-8608            Impact factor:   2.574


  31 in total

1.  pH-dependent solubility shift of rubella virus capsid protein.

Authors:  C A Mauracher; S Gillam; R Shukin; A J Tingle
Journal:  Virology       Date:  1991-04       Impact factor: 3.616

2.  X-ray solution scattering of Sindbis virus. Changes in conformation induced at low pH.

Authors:  M J Stubbs; A Miller; P J Sizer; J R Stephenson; A J Crooks
Journal:  J Mol Biol       Date:  1991-09-05       Impact factor: 5.469

3.  Semliki Forest virus envelope proteins function as proton channels.

Authors:  A Schlegel; A Omar; P Jentsch; A Morell; C Kempf
Journal:  Biosci Rep       Date:  1991-10       Impact factor: 3.840

4.  Low pH-induced cell fusion in flavivirus-infected Aedes albopictus cell cultures.

Authors:  V B Randolph; V Stollar
Journal:  J Gen Virol       Date:  1990-08       Impact factor: 3.891

5.  Identification of a region in the Sindbis virus nucleocapsid protein that is involved in specificity of RNA encapsidation.

Authors:  K E Owen; R J Kuhn
Journal:  J Virol       Date:  1996-05       Impact factor: 5.103

6.  Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa.

Authors:  H Schägger; G von Jagow
Journal:  Anal Biochem       Date:  1987-11-01       Impact factor: 3.365

7.  Deletion analysis of the capsid protein of Sindbis virus: identification of the RNA binding region.

Authors:  U Geigenmüller-Gnirke; H Nitschko; S Schlesinger
Journal:  J Virol       Date:  1993-03       Impact factor: 5.103

8.  Isolation of a Singh's Aedes albopictus cell clone sensitive to Dengue and Chikungunya viruses.

Authors:  A Igarashi
Journal:  J Gen Virol       Date:  1978-09       Impact factor: 3.891

9.  Inhibition of Semliki forest virus penetration by lysosomotropic weak bases.

Authors:  A Helenius; M Marsh; J White
Journal:  J Gen Virol       Date:  1982-01       Impact factor: 3.891

10.  Effect of weak bases on the intralysosomal pH in mouse peritoneal macrophages.

Authors:  B Poole; S Ohkuma
Journal:  J Cell Biol       Date:  1981-09       Impact factor: 10.539

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  1 in total

Review 1.  Tissue Barriers to Arbovirus Infection in Mosquitoes.

Authors:  Alexander W E Franz; Asher M Kantor; A Lorena Passarelli; Rollie J Clem
Journal:  Viruses       Date:  2015-07-08       Impact factor: 5.048

  1 in total

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