Abstract
The alphavirus capsid protein (CP) binds to viral genomic RNA to form cytoplasmic nucleocapsid cores, and these cores interact with the cytoplasmic domain of the E2 glycoprotein (cdE2) as particles bud from the plasma membrane. Button and Mukhopadhyay (e01062-21) show that changing the length and/or charge of the CP can abolish cytoplasmic core formation. However, even if cytoplasmic cores are not formed, cdE2-CP interactions are sufficient to mediate core assembly inside released virions. These results show the virus has multiple mechanisms in place to package the viral genome.
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