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.
Cielens
I
I
Biomedical Research and Study Centre, University of Latvia, 1 Ratsupites Street, LV-1067, Riga, Latvia.
Ose
V
V
Petrovskis
I
I
Strelnikova
A
A
Renhofa
R
R
Kozlovska
T
T
Pumpens
P
P
D017908:Allolevivirus / Q000737:chemistry* / Q000235:genetics / Q000276:immunology / Q000648:ultrastructure; D000595:Amino Acid Sequence; D003545:Cysteine / Q000737:chemistry / Q000235:genetics; D005822:Genetic Vectors; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D012367:RNA, Viral / Q000737:chemistry / Q000235:genetics; D017386:Sequence Homology, Amino Acid; D014771:Virion / Q000737:chemistry* / Q000276:immunology / Q000648:ultrastructure
D012367:RNA, Viral; D003545:Cysteine