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...

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Veröffentlicht in:	FEBS letters 2000-10, Vol.482 (3), p.261
Hauptverfasser:	Cielens, I, Ose, V, Petrovskis, I, Strelnikova, A, Renhofa, R, Kozlovska, T, Pumpens, P
Format:	Artikel
Sprache:	eng
Schlagworte:	Allolevivirus - chemistry Allolevivirus - genetics Allolevivirus - immunology Allolevivirus - ultrastructure Amino Acid Sequence Cysteine - chemistry Cysteine - genetics Genetic Vectors Molecular Sequence Data Mutagenesis, Site-Directed RNA, Viral - chemistry RNA, Viral - genetics Sequence Homology, Amino Acid Virion - chemistry Virion - immunology Virion - ultrastructure
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Zusammenfassung:	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.
ISSN:	0014-5793