6533b822fe1ef96bd127d6c9

RESEARCH PRODUCT

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

Tatyana KozlovskaRegina RenhofaIndulis CielensVelta OseAnna StrelnikovaPaul PumpensIvars Petrovskis

subject

Icosahedral symmetryvirusesGenetic VectorsMolecular Sequence DataBiophysicsBiologymedicine.disease_causecomplex mixturesBiochemistryVirus-like particleStructural BiologyGeneticsmedicineAmino Acid SequenceCysteineMolecular BiologyEscherichia coliPeptide sequenceIcosahedronAlloleviviruschemistry.chemical_classificationSequence Homology Amino AcidRod-like structureVirionvirus diseasesRNASelf-assemblyCell Biologybiochemical phenomena metabolism and nutritionAmino acidCrystallographyCapsidchemistryMutagenesis Site-DirectedRNA ViralRNA phage QβVirus-like particleCysteine

description

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.

yearjournalcountryeditionlanguage
2000-10-12FEBS Letters
https://doi.org/10.1016/s0014-5793(00)02061-5