Semliki Forest virus nucleocapsid

Soderlund, H. (1973). Kinetics of formation of Semliki Forest virus nucleocapsid. Intervirology 1, 354-361. 

The diminution in infectivity could be caused either by the production of virus particles having a lessened or abolished infectivity, or a decreased formation of infectious virions. The envelope glycoproteins of Semliki Forest virus and Sindbis virus synthesized in the presence of tunicamycin (and, thus, devoid of carbohydrate) are metabolically stable. They do not participate in the assembly of virus particles, although nucleocapsids are still formed under these conditions and are... 

Metsikko, K., and Garoff, H. (1990). Oligomers of the cytoplasmic domain of the p62/ E2 membrane protein of Semliki Forest virus bind to the nucleocapsid in vitro. J. Virol 64, 4678-4683. 

The stepwise dissociation of the Semliki Forest (SF) Viral membrane with Triton X-100 [82] has been described. The SF virus has one of the simplest biological membranes it has a spherical nucleocapsid consisting of RNA and one polypeptide. The nucleocapsid is surrounded by a lipid-protein membrane similar in composition to that of the host cell plasma membrane as it acquires this protective layer by budding as it leaves the cell. Binding of Triton to the membrane occurs below the CMC and increases with increasing surfactant concentration. Release of the nucleocapsids from the virus occurs when more than 0.2 to 0.4 mg Triton is bound per mg membrane. When higher concentrations of Triton were present (c 1.6 mg bound) the membranes dissociate to protein-lipid-surfactant complexes, followed at higher surfactant concentrations by delipidation of membrane protein (see Fig. 10.13). Lipophilic proteins isolated... 

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