The reaction of EEE virus preparations with sodium deoxycholate

Richter, Alan; Wecker, Eberhard

doi:10.1016/0042-6822(63)90114-4

Cited by 26 publications

(9 citation statements)

References 8 publications

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“…Group A arbovirus virions consist of a nucleocapsid tightly wrapped in a lipid-containing envelope (1, 11). The RNA within complete virions of several group A arboviruses is resistant to ribonuclease digestion (12,15,18), although, as in Semliki Forest virus, their nucleocapsids are ribonuclease-sensitive (5,16,17). Thus, the envelope protects the viral RNA within the nucleocapsid from enzymatic attack.…”

Section: IImentioning

confidence: 99%

Ribonuclease Sensitivity of Semliki Forest Virus Nucleocapsids

Acheson

Tamm

1970

J Virol

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Section: IImentioning

confidence: 99%

Ribonuclease Sensitivity of Semliki Forest Virus Nucleocapsids

Acheson

Tamm

1970

J Virol

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“…Ribonuclease tests, not included into the Tables, proved that the infectivity measured was destroyed by this enzyme and that infectious RNA did not interfere with the virus plaque-forming-units assay. Almost all the virus infectivity was destroyed by the deoxycholate treatment (Richter & Wecker, 1963 ;Osterrieth, 1964). When the caseinase C treatment destroyed a significant proportion of the infectivity, the p.f.u.:RNA-p.f.u.…”

Section: Virus Infectious Titre To the Deoxycholate-liberated R N A Imentioning

confidence: 99%

“…Deoxycholate-treated virus and controls were also incubated in presence of ribonuclease (0-6 pg./ml.). The assay of these suspensions was done according to the method of Richter & Wecker (1963). The deposit of the overlay, the following incubation and the staining were done as described in the preceding paragraph.…”

Section: Introductionmentioning

confidence: 99%

Changes in Morphology, Infectivity and Haemagglutinating Activity of Semliki Forest Virus Produced by the Treatment with Caseinase C from Streptomyces albus G.

Osterrieth

Calberg-Bacq

1966

Journal of General Microbiology

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SUMMARYElectron micrographs of negatively stained Semliki Forest virus were made before and after treatment of the virus with caseinase C from Strqtmyces altncs G. The virus appeared as roughly spherical (diameter 550-590 a); covered with projections and sometimes bearing an appendix, which seemed to be a fold of the envelope. Treated with caseinase C in tris buffered saline, the virus lost its projections and its haemagglutinating activity but remained infectious. The site of haemagglutination, then, is probably located on the projections. Treated with caseinase C in phosphate buffer, the virus lost its infectivity as well as its haemagglutinating activity; the number of the remaining viral particles was not significantly modified. These structures had no projections; their envelope was degraded and sometimes completely destroyed. In this case, they had a smaller diameter (885-890 a) than the projectionless particles obtained by treatment in tris buffered saline (410460a). As the virus particles with degraded envelope still contained as much infectious RNA as the controls, it was thought that some degree of integrity of the envelope was necessary for the particle infectivity. Thus the site for infectivity appeared to be different from that for haemagglutination.

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“…Assay of infectious RNA. Infectious RNA was assayed by the plaque technique on CE cells which had been washed with hypertonic saline (16).…”

mentioning

confidence: 99%

Maturation Defects in Temperature-sensitive Mutants of Sindbis Virus

Yin

Lockart

1968

J Virol

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Temperature-sensitive mutants of Sindbis virus, which synthesize viral ribonucleic acid (RNA) but not mature virus at the nonpermissible temperature, were selected for the study of viral maturation. Of these, three mutants which complement each other genetically were used. Two major proteins, the nucleocapsid and membrane proteins, located, respectively, in the viral nucleoid and membrane, were found in intact virions. In cells infected with wild-type Sindbis virus, four distinct types of viral RNA with sedimentation coefficients of 40S, 26S, 20S, and 15S were detected in constant distribution. The 20S RNA was ribonuclease-resistant, whereas the other types were ribonuclease-sensitive. The 40S RNA, identical to that obtained from the virion, was found associated with nucleocapsid protein as a subviral particle, which was assumed to be the nucleoid. Viral materials from cells infected with the mutants under nonpermissive conditions were compared with those from cells infected with wild-type virus, in terms of (i) the distribution of the different types of RNA, (ii) the association of infectious viral RNA into subviral particles, and (iii) the ability of infected cells to hemadsorb goose erythrocytes. According to these criteria, each of the three mutants demonstrated different maturation defects. Defective nucleocapsid proteins and membrane proteins may each account for one of the above mutants. The third mutant may have defects in a minor structural protein or possibly a maturation protein which is involved in the assembly of Sindbis virus.

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The reaction of EEE virus preparations with sodium deoxycholate

Cited by 26 publications

References 8 publications

Ribonuclease Sensitivity of Semliki Forest Virus Nucleocapsids

Ribonuclease Sensitivity of Semliki Forest Virus Nucleocapsids

Changes in Morphology, Infectivity and Haemagglutinating Activity of Semliki Forest Virus Produced by the Treatment with Caseinase C from Streptomyces albus G.

Maturation Defects in Temperature-sensitive Mutants of Sindbis Virus

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