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Mutilation of RNA phage Qbeta virus-like particles: from icosahedrons to rods.

Icosahedral virus-like particles (VLPs) of RNA phage Qbeta are stabilized by four disulfide bonds of cysteine residues 74 and 80 within the loop between beta-strands F and G (FG loop) of the monomeric subunits, which determine the five-fold and quasi-six-fold symmetry contacts of the VLPs. In order to reduce the stability of Qbeta VLPs, we mutationally converted the amino acid stretch 76-ANGSCD-81 within the FG loop into the 76-VGGVEL-81 sequence. It led to production in Escherichia coli cells of aberrant rod-like Qbeta VLPs, along with normal icosahedral capsids. The length of the rod-like particles exceeded 4-30 times the diameter of icosahedral Qbeta VLPs.[1]

References

  1. Mutilation of RNA phage Qbeta virus-like particles: from icosahedrons to rods. Cielens, I., Ose, V., Petrovskis, I., Strelnikova, A., Renhofa, R., Kozlovska, T., Pumpens, P. FEBS Lett. (2000) [Pubmed]
 
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