| Literature DB >> 11024472 |
I Cielens1, V Ose, I Petrovskis, A Strelnikova, R Renhofa, T Kozlovska, P Pumpens.
Abstract
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.Entities:
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Year: 2000 PMID: 11024472 DOI: 10.1016/s0014-5793(00)02061-5
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124