Disease relevance of RNA Phages

• By use of Q beta RNA phage as a model system, the effect of an antiviral gene therapy, i.e., a virus-specific repressor protein expressed by a recombinant Escherichia coli host, was studied over the course of more than 100 generations [1].
• From these in vitro results, the role of the polyamine spermidine in the RNA phage particle for the infecting, RNA-A protein complex molecules in phage infection is discussed [2].
• These results validate RNA phage capsid display of immunogenic determinants as a basis for the development of novel peptide vaccines and indicate that further evaluation of MS2 coat protein as a vector for malaria epitopes is merited [3].
• Adsorption of the isometric RNA phage MS2 to R711b pili occurs in the presence but not in the absence of formalin, which presumably prevents elution of reversibly adsorbed virions [4].

High impact information on RNA Phages

• Overlapping genes in RNA phage: a new protein implicated in lysis [5].
• This contrasts with the situation in the distantly related group I RNA phages such as f2 and MS2 where a small lysis polypeptide is coded for by a region overlapping the end of the coat gene and the beginning of the replicase gene [6].
• RNA packaging device of double-stranded RNA bacteriophages, possibly as simple as hexamer of P4 protein [7].
• The coat proteins of RNA phages MS2 and GA are specific RNA-binding proteins which function to encapsidate viral RNA and to translationally repress synthesis of the viral replicase [8].
• Rescue of the RNA phage genome from RNase III cleavage [9].

Chemical compound and disease context of RNA Phages

• Effect of spermidine on the RNA-A protein complex isolated from the RNA bacteriophage MS2 [2].
• 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 [10].
• Streptomycin administration gradually led to the disappearance of bacteria and, concomitantly, the RNA phages [11].
• In vitro transcription of the double-stranded RNA bacteriophage phi 6 is influenced by purine NTPs and calcium [12].
• A terminal 2 kb EcoRI-BamHI fragment from pRA300 complemented the chromosomal cpxA2[Ts] allele with respect to isoleucine and valine synthesis, RNA bacteriophage sensitivity and surface exclusion in Hfr strains, and envelope protein composition [13].

Biological context of RNA Phages

• Conjugation system of IncC plasmid RA1, and the interaction of RA1 pili with specific RNA phage C-1 [14].
• Sequence-specific interactions between RNA stem-loops and coat protein (CP) subunits play vital roles in the life cycles of the RNA bacteriophages, e.g., by allowing translational repression of their replicase cistrons and tagging their own RNA genomes for encapsidation [15].
• Both the statistical analyses and the studied predictive models indicate that genotype II of F-specific RNA bacteriophages, the coprostanol and the ratio coprostanol: coprostanol+epicoprostanol are, out of the studied parameters, those with a greater discriminating power [16].

Anatomical context of RNA Phages

• Some balloon-like structures also appeared on the surfaces of cells induced by the cloned lysis gene of RNA phage SP and material also appeared to be leaking through the cell wall in the photographs [17].

Gene context of RNA Phages

• RNA phage KU1 has an insertion of 18 nucleotides in the start codon of its lysis gene [18].
• The high flexibility of the C-terminal region of VP1 was confirmed by the formation of chimeric virus-like particles based on the coat protein of the RNA bacteriophage fr which was previously found to tolerate only very short-sized foreign insertions [19].
• HF-I is a small, heat-stable, site-specific RNA-binding protein originally characterized for its role in replication of the RNA bacteriophage Q beta of E. coli [20].
• MS2 is an RNA bacteriophage (3569 bases) [21].
• The RNA polymerase complex of double-stranded RNA bacteriophage phi6 is composed of four proteins, P1, P2, P4 and P7 [22].

References