Adenovirus fiber

Fig. 2. Adenovirus fiber head domain. (A) Adenovirus type 12 fiber head seen from the side (PDB-code 1NOB Bewley et al., 1999). The three monomers are colored differendy. (B) Adenovirus type 12 fiber head domain bound to CAR D1 seen from the top (PDB-code 1KAC Bewley et al., 1999). Here, the adenovirus type 12 trimer is shown in yellow and the CAR D1 domain in purple. Figures 2-5 were produced using PyMOL (DeLano, 2002).

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).

Burmeister, W. P., Guilligay, D., Cusack, S., Wadell, G., and Amberg, N. (2004). Crystal structure of species D adenovirus fiber knobs and their sialic acid binding sites. J. Virol. 78, 7727-7736. 

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. 

Lortat-Jacob, H., Chouin, E., Cusack, S., and van Raaij, M.J. (2001). Kinetic analysis of adenovirus fiber binding to its receptor reveals an avidity mechanism for trimeric receptor-ligand interactions./. Biol. Chem. 276, 9009-9015. 

Papanikolopoulou, K., Forge, V., Goeltz, P., and Mitraki, A. (2004a). Formation of highly stable chimeric trimers by fusion of an adenovirus fiber shaft fragment with the foldon domain of bacteriophage t4 fibritin. /. Biol. Chem. 279, 8991-8998. 

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. 

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 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... 

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). 

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

Nicklin S A, Wu E, Nemerow G R, et al. (2005). The influence of adenovirus fiber structure and function on vector development for gene therapy. Molec. Ther. 12 384-393. 

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

The receptor ligand transferrin has been incorporated into chitosan/DNA polyplexes which enhanced gene transfer up to four-fold compared to immod-ified chitosan [67]. In a similar fashion, incorporation of C-terminal domain of adenovirus fiber knob protein enhanced transfection up to 130-fold in HeLa cells. Further modifications include the incorporation of hydrophobic moieties to generate dodecylated chitosan, deoxychoHc acid modified chitosan. Urocanic acid-modified chitosan [68] was reported to mediate efficient gene delivery it was hypothesized that the imidazole ring plays a crucial role for enhancing the release of internalized polyplexes from endosomal vesicles. 

The structural proteins of AAV particles have been dissociated with sodium dodecyl sulfate (SDS) or urea and then separated by polyacrylamide gel electrophoresis (Johnson and Hoggan, 1971 Rose et al., 1971). Three proteins were identified with estimated molecular weights of 62-66000 73-80000 and 87-92000, respectively. The smallest polypeptide represented about 80% of the total protein mass while the other two represented approximately 10% each. There was no correspondence in electrophoretic mobility with adenovirus structural proteins except that there was a partial overlap of the major AAV protein and the adenovirus fiber penton. The three AAV capsid proteins were present in all three human serotypes (AAV I-3) and had similar mobilities with the exception that the major protein species of AAV 2 moved slightly faster than the comparable AAV 1 and 3 species. Very minor... 

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