Microviridae

Microviridae is a family of bacteriophages with a single-stranded DNA genome. The name of this family is derived from the ancient Greek word μικρός (mikrós), meaning 'small'. This refers to the size of their genomes, which are among the smallest of the DNA viruses. Enterobacteria, intracellular parasitic bacteria, and spiroplasma serve as natural hosts. There are currently 12 species in this family, divided among 7 genera and one subfamily. The virons are non-enveloped, round with an icosahedral symmetry (T = 1). They have a diameter between 25–27 nanometers and lack tails. Each viron has 60 copies each of the F, G, and J proteins and 12 copies of the H protein. They have 12 pentagonal trumpet-shaped pentamers (~7.1 nm wide × 3.8 nm high), each of which composed of 5 copies of G and one of the H protein. Viruses in this family replicate their genomes via a rolling circle mechanism and encode dedicated RCR initiation proteins. Although the majority of species in this family have lytic life cycles, a few may have temperate life cycles. The genome sizes range from 4.5–6kb and is circular. It encodes 11 genes (in order: A, A*, B, C, K, D, E, J, F, G, and H), nine of which are essential. The nonessential genes are E and K. Several of the genes have overlapping reading frames. Protein A* is encoded within protein A. It lacks ~1/3 of the amino acids from the N terminal of the A protein and is encoded in the same frame as the A protein. It is translated from an internal start site within the messenger RNA. Gene E is encoded with gene D with a +1 frameshift. Gene K overlaps genes A, B, and C. The origin of replication lies within a 30 base sequence. The entire 30 base sequence is required for replication. The major capsid protein (F) has 426 amino acids, the major spike protein (G) has 175 amino acids, the small DNA-binding protein (J) has 25–40 amino acids, and the DNA pilot protein (H) has 328 amino acids. The major folding motif of protein F is the eight-stranded antiparallel beta barrel common to many viral capsid proteins. The G protein is a tight beta barrel with its strands running radially outward. The G proteins occur in groups of five forming 12 spikes that enclose a hydrophilic channel. The highly basic J protein lacks any secondary structure and is situated in an interior cleft of the F protein. It has no acidic amino acid residues in the protein and the twelve basic residues are concentrated in two clusters in the N-terminus separated by a proline-rich region. Assembly of the virion uses two scaffolding proteins, internal scaffolding protein B and external scaffolding protein D. The function of protein B seems to be to lower the amount of protein D needed by the virion for assembly. Protein H is a multifunctional structural protein required for piloting the viral DNA into the host cell interior during the entry process. Protein E is a 91-amino acid membrane protein that causes host cell lysis by inhibiting the host translocase MraY. This inhibitory activity is located within the N terminal 29 amino acids. Protein A is a single strand endonuclease and is responsible for the initiation of viral DNA replication. It catalyses cleavage and ligation of a phosphodiester bond between a G and A nucleotide residue pair at the phi X origin. It may not be essential for phage viability but burst sizes are reduced by 50% when it is mutated. Protein A* inhibits host DNA replication. Unlike protein A it is capable of cleaving the phi X viral DNA in the presence of single-stranded binding protein of the host. Protein A*, like Protein A, may not be required for phage viability. Protein C increases the fidelity of the termination and reinitiation reactions and is required for the packagaging of the viral DNA in to the protein shell. Protein K has 56 amino acids and is found in the membrane of the host cell. It appears to be able to increase the burst size of the virus. Group: ssDNA