Self-assembly of viral capsid protein and RNA molecules of different sizes: requirement for a specific high protein/RNA mass ratio
|Title||Self-assembly of viral capsid protein and RNA molecules of different sizes: requirement for a specific high protein/RNA mass ratio|
|Publication Type||Journal Article|
|Year of Publication||2011|
|Authors||Cadena-Nava, RD, Comas-Garcia, M, Garmann, RF, Rao, ALN, Knobler, CM, Gelbart, WM|
|Journal||Journal of Virology|
Virus-like particles (VLPs) can be formed by self-assembly of capsid protein (CP) with RNA molecules of increasing length. If the protein “insisted” on a single radius of curvature, the capsids would be identical in size, independent of RNA length. But there would be a limit to length of the RNA, and one would not expect RNA much shorter than native viral RNA to be packaged unless multiple copies were packaged. On the other hand, if the protein did not favor pre-determined capsid size, one would expect the capsid diameter to increase with increase in RNA length. Here we examine the self-assembly of CP from cowpea chlorotic mottle virus (CCMV) with RNA molecules, ranging in length from 140 to 12,000 nucleotides (nt). Each of these RNAs is completely packaged if and only if the protein:RNA mass ratio is sufficiently high; this critical value is the same for all the RNAs, and corresponds to equal RNA and N-terminal-protein charges in the assembly mix. For RNAs much shorter in length than the 3000 of the viral RNA, two or more molecules are assembled into 24-nm and 26-nm diameter capsids while for much longer RNAs (>4500nt) a single RNA molecule is shared/packaged by two or more capsids with diameters as large as 30 nm. For intermediate lengths a single RNA is assembled into 26-nm diameter capsids, the size associated with T = 3 wildtype virus. The significance of these assembly results is discussed in relation to likely factors that maintain T=3 symmetry in vivo.