Structural protein of cauliflower mosaic virus

Tezuka, Nobuo; Taniguchi, Takeshi

doi:10.1016/0042-6822(72)90143-2

Cited by 12 publications

(3 citation statements)

References 14 publications

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“…of 27, 32, 40, 67, 92 and IOO × Io ~, the last two of which were glycopeptides. We report here the amino acid composition of the total virus protein and results which indicate that C1MV is structurally more complex than reported by Tezuka & Taniguchi (1972b) but less complex than proposed by Kelly et al (1974).…”

Section: The Composition Of Cauliflower Mosaic Virus Proteinmentioning

confidence: 67%

The Composition of Cauliflower Mosaic Virus Protein

Brunt¹,

Barton²,

Tremaine

et al. 1975

Journal of General Virology

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Section: The Composition Of Cauliflower Mosaic Virus Proteinmentioning

confidence: 67%

The Composition of Cauliflower Mosaic Virus Protein

Brunt¹,

Barton²,

Tremaine

et al. 1975

Journal of General Virology

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“…Tipula iridescent virus was found to contain 28 polypeptides ranging in molecular weight from 17.5 to 300 x 10 3 ; none was a glycoprotein (Krell and Lee, 1974). In keeping with their small size, plant ICDVs have a simple electrophoretic profile of protein; cauliflower mosaic virus contains only two structural proteins, having molecular weights of 68,000 and 33,000 (Tezuka and Taniguchi, 1972).…”

Section: Proteinsmentioning

confidence: 97%

Icosahedral Cytoplasmic Deoxyriboviruses

Goorha

Granoff

1979

Comprehensive Virology

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“…None of these proteins reacted with Schiff's reagent, suggesting the absence of a glycoprotein in these viruses. The smaller cauliflower mosaic virus has been reported to have only two structural proteins (Tezuka & Taniguchi 1972). Therefore it may be justifiable to place PM2 in the ICDV group.…”

Section: S Ome Other Viruses W Ith N O V O Assembly Of the Lipid Componentsmentioning

confidence: 99%

Structure and assembly of lipid-containing viruses, with special reference to bacteriophage PM2 as one type of model system

Franklin

Hinnen

Tsukagoshi

1976

Phil. Trans. R. Soc. Lond. B

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The simpler lipid-containing viruses (influenza, Semliki Forest, PM2) may have a phospholipid bilayer sandwiched between an outer shell of protein and an internal nucleocapsid possessing helical or icosahedral symmetry. Extensive physical and chemical studies have enabled us to form a more detailed picture of the structure of bacteriophage PM2 and controlled stepwise degradation of the virion has helped us to localize the four viral proteins. The surface protein (II) of PM2 is basic and interacts with the acidic phosphatidylglycerol of the bilayer to stabilize the membrane. The nucleocapsid protein (III) has proteolipid characteristics and may interact with the phospholipids in a hydrophobic fashion. The spikes are formed from protein I and the fourth protein (IV) is closely associated with the DNA. It is possible to reassemble the virus by reversing the degradation steps. Assembly has been especially useful in revealing the processes whereby the proteins and lipids interact to form the bilayer. Furthermore, results of in vivo studies of phospholipid synthesis and both in vivo and in vitro studies of viral protein synthesis have enabled us to form a reasonably complete picture of the biosynthesis of PM2.

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Structural protein of cauliflower mosaic virus

Cited by 12 publications

References 14 publications

The Composition of Cauliflower Mosaic Virus Protein

The Composition of Cauliflower Mosaic Virus Protein

Icosahedral Cytoplasmic Deoxyriboviruses

Structure and assembly of lipid-containing viruses, with special reference to bacteriophage PM2 as one type of model system

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