Adenovirus core protein VII displays a linear epitope conserved in a range of human adenoviruses.

Abstract

Adenoviruses (Ads) have a complex architecture with at least 12 structural proteins. The major protein, the hexon, is the main component of the capsid and there are a number of other capsomeres which complete the capsid and link with the core of the virus (Stewart et al., 1993). The latter consists of the viral double-stranded DNA genome in association with a number of other proteins -the principal ones being proteins VII and V as well as the small peptide mµ. The spatial organization of the core has been the subject of a number of studies, sometimes with conflicting conclusions (for reviews see Nermut, 1984 ;Vayda et al., 1983). Protein VII is a highly basic protein very tightly attached to the viral DNA and most likely plays a role analogous to histones in cellular chromatin. However, very little is known of its structure and function although some

Adenovirus core protein VII contains distinct sequences that mediate targeting to the nucleus and nucleolus, and colocalization with human chromosomes

“…Whilst adenovirus core protein VII has been proposed to fulfil a histone-like role in condensing adenovirus DNA (Sung et al, 1983), this is the first report of protein VII colocalizing with human chromosomes. The possible significance of this colocalization remains to be explored; however, it is notable that other than the precursor fragment 1-24, the sequence 25-54 which colocalizes with chromosomes is the most highly conserved sequence between human, canine and mouse adenoviruses (Tarassishin et al, 1999), and shares some similarity with the N-terminal regulatory tail of histone H3 (Fig. 3B), a region responsible for transcriptional control (Cai & Weber, 1993;Strahl & Allis, 2000).…”

“…Antibodies raised against protein Mu for use in Western blots and ELISA cross-react with protein VII, presumably due to the homologous unusual arginine-rich sequences present in both proteins (Lunt et al, 1988). Protein VII has homologues in every adenovirus studied so far isolated either from mammals and birds, or from lower vertebrates (Zhang et al, 1991;Tarassishin et al, 1999;Farkas et al, 2002;Davison et al, 2003), and has significant functional and sequence similarity with histone H3 (Cai & Weber, 1993). Whether protein VII has any role beyond that of a DNA-binding protein remains unclear, but protein VII enhances the uptake and expression of naked DNA fourfold when used as a transfection adjuvant for mammalian cells (Wienhues et al, 1987), suggesting that it may be actively involved in the transport of DNA to the nucleus.…”

Characterization and manipulation of the human adenovirus 4 genome

“…HAdV-4 strains can be differentiated into two groups on the basis of minor differences in restriction endonuclease digest patterns; the prototype strain [RI-67, deposited in the American Type Culture Collection (ATCC) as VR-4] and vaccine strain (CL 68578) are members of the same group (Li & Wadell, 1988). DNA sequence data are available for several loci in a variety of HAdV-4 strains (Tokunaga et al, 1982(Tokunaga et al, , 1986Hay, 1985;Kitchingman, 1985;Gruber et al, 1993;Kidd et al, 1995;Crawford-Miksza et al, 1999;Tarassishin et al, 1999;Li & Wold, 2000). Here, we report the complete DNA sequence of the vaccine strain, thus defining a therapeutic agent and enabling researchers to access a genome sequence for at least one human adenovirus from each of the six species.…”