Adenovirus, fiber proteins

Zhang, F., Andreassen, P., Fender, P., Geissler, E., Hernandez, J.H. and Chroboczek, J. (1999) A transfecting peptide derived from adenovirus fiber protein. Gene Then, 6, 171-181. 

The adenovirus fiber protein is trimeric, and the monomer varies in length from 320 to 587 residues (Chroboczek et al, 1995). The N-terminal region of the fiber protein associates with the penton base protein in the... 

Adenovirus fiber protein [81] Many trypanosome proteins [Kelly and Hart,... 

Micheal, S.I. et al.. Addition of a short peptide Kgand to the adenovirus fiber protein. Gene Ther., 2,660,1995. 

Macejak, D.G. Luftig, R.B. (1991). Association of Hsp70 with the adenovirus type 5 fiber protein in infected Hep-2 ceils. Virology 180, 120-125. 

Fig. 1. Schematic drawings of the viruses discussed in this chapter. (A) An icosahe-dral virus with fiber proteins inserted in its pentameric vertices. The gray box denotes domains with known structures for adenovirus, reovirus, and bacteriophage PRD1, in each case containing the head domain and proximal part of the triple /8-spiral shaft domain. (B) Contractile-tailed bacteriophage T4. T4 contains three different fibrous proteins, fibritin connected to the neck, the long (bent) fibers connected to the base plate, and the short fibers also connected to the base plate. Only two of each of the trimeric fibrous proteins are shown for clarity. The gray box denotes domains with known structure for the T4 short fiber.

Fig. 3. Structure and sequence of repeats present in the fibrous proteins discussed in this chapter. (A) The adenovirus triple -spiral. A single repeat of one of the chains is shown as a stick model colored by atom, the other two as a secondary structure cartoon in yellow and orange. Amino acids contributing to the hydrophobic core are labeled, as is the glycine in the turn. (B) Triple -spiral sequence repeats. Conserved hydrophobic residues are indicated by a hash sign, the conserved glycine or proline by an asterisk. (C) The T4-hber fold. A single repeat of one of the chains is shown as a stick model colored by atom, the other two as a secondary structure cartoon in yellow and orange. Several of the conserved amino acids are labeled. (D) Repeating sequences present in bacteriophage T4 fiber proteins (Cerritelli et al., 1996). Conserved amino acids are indicated by a small letter conserved hydrophobic residues by a hash sign, and conserved small amino acids by a dot.

Fig. 5. The triple //-spiral in the adenovirus fiber shaft. (A) The triple //-spiral domain alone. Shown are amino acids 319-392 of each of the three chains, forming four triple /1-spiral repeats (van Raaij et al, 1999b). (B) Structure of a chimeric adenovirus fiber shaft-fibritin foldon domain protein (Papanikolopoulou et al, 2004b).

Chappell, J. D., Prota, A. E., Dermody, T. S., and Stehle, T. (2002). Crystal structure of reovirus attachment protein sigmal reveals evolutionary relationship to adenovirus fiber. EMBOJ. 21, 1-11. 

Krasnykh, V., Belousova, N., Korokhov, N., Mikheeva, G., and Curiel, D. T. (2001). Genetic targeting of an adenovirus vector via replacement of the fiber protein with the phage T4 fibritin./ Virol. 75, 4176-4183. 

Papanikolopoulou, K., Schoehn, G., Forge, V., Forsyth, V. T., Riekel, C., Hernandez, J.-F., Ruigrok, W. H., and Mitraki, A. (2005). Amyloid fibril formation from sequences of a natural jS-structured fibrous protein, the adenovirus fiber. J. Biol. Chem. 280, 2481-2490. 

Xia, D., Henry, L.J., Gerard, R. D., and Deisenhofer, J. (1994). Crystal structure of the receptor-binding domain of adenovirus type 5 fiber protein at 1.7 A resolution. Structure 2, 1259-1270. 

R. Gonzalez, R. Vereecque, T. J. Wickham, M. Vanrumbeke, I. Kovesdi, F. Bau-ters, P. Fenaux, and B. Quesnel, Increased gene transfer in acute myeloid leukemic cells by an adenovirus vector containing a modified fiber protein, Gene Ther. 6 314 (1999). 

More recently the crystal structures of the adenovirus fiber shaft and receptor-binding fiber head (van Raaij et al, 1999) and of the head in complex with the coxsackie-adenovirus receptor molecule (GAR) (Bewley et al, 1999) have been solved. The fiber shaft structure revealed a novel (3-sheet triple spiral fold, which is perhaps particularly suited to forming rigid protein projections for interaction with and penetration through cell membranes by adenovirus the structure of the complex that performs the same function in bacteriophage T4 has been solved, revealing a similar fold (Kanamaru et al, 2002). 

The primary cellular attachment receptor for adenovirus has not yet been identified, but the vitronectin-binding integrins Oy/Sj and Oy/ s have been shown to be coreceptors for viral internalization [113] and interact with the penton base of the capsid. It is thought that the initial interaction with the cell surface is mediated by the protruding fiber proteins. The various subgroups presumably bind to different receptors because they do not compete with one another for cellular binding. Subsequent interactions between the Oy coreceptors and the penton base... 

P2 (left) domains are antiparallel eight-stranded fi barrels. The connecting domain and intertwined loops hold them together. The coloring of both jelly-roll domains is as in Fig. 1. (b) The P3 m or capsid protein of bacteriophage PRDl (Benson et al, 1999) with the same coloring scheme, (c) The knob domain of the adenovirus fiber (van Raaij et al, 1999b). (d) Part of the trimeric adenovirus type 2 fiber, vdth 4 of the 15-residue repeats (total, 22 in this strain). 

Plum pox virus capsid protein Baculovirus gp41 tegument protein HCMV UL32 (BPP) tegument protein NS26 rotavirus protein SV-40 large T antigen Virion basic phosphoprotein Adenovirus type 2 fiber protein Adenovirus type 5 fiber protein... 

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