Virus capsid proteins

NT070 Mason, H. S., J. M. Ball, J. J. Shi, X. Jiang, M. K. Estes, and C. J. Amtzen. Expression of Norwalk virus capsid protein in transgenic tobacco and potato and its oral immunogenicity in mice. Proc Natl Acad Sci USA 1996 93(11) 5335-5340. 

Martin-Alonso, J.M., Castanon, S., Alonso, R, Parra, E, and Ordas, R. (2003). Oral immunization nsing tuber extracts from transgenic potato plants expressing rabbit hemorrhagic disease virus capsid protein. Transgenic Res. 12 127-130. 

Zhang, X., Buehner, N.A., Hutson, A.M., Estes, M.K., and Mason, H.S. (2006). Tomato is a highly effective vehicle for expression and oral immunization with Norwalk virus capsid protein. Plant Biotechnol J. 4(4) 419 32. 

A certain class of virus capsides (protein shells of virions) have a spherical structure, that is modeled on dual GCk,i(Dodecahedron) (see [CaK162, Cox71, DDG98]). 

Wang MY, Kuo YY, Lee MS, Doong SR, Ho JY, Lee LH (2000), Self-assembly of the infectious bursal disease virus capsid protein, rVP2, expressed in insect cells and purification of immunogenic chimeric rVP2H particles by immobilized metal-ion affinity chromatography, Biotechnol. Bioeng. 67 104-111. 

Aliperti, G., and Schlesinger, M. J. (1978). Evidence for an autoprotease activity of Sindbis virus capsid protein. Virology 90, 366-369. 

Glanville, N., and Ulmanen, J. (1976). Biological activity of in vitro synthesized protein Binding of Semliki Forest virus capsid protein to the large ribosomal subunit. Biochem. Biophys. Commun. 71, 393-399. 

Hahn, C. S., and Strauss, J. H. (1990). Site-directed mutagenesis of the proposed catalytic amino acids of the Sindbis virus capsid protein autoprotease. J. Virol. 64, 3069-3073. 

Soderlund, H., and Ulmanen, I. (1977). Transient association of Semliki Forest virus capsid protein with ribosomes. J. Virol. 24, 907-909. 

Coombs, K., and Brown, D. T. (1987). Topological organization of Sindbis virus capsid protein in isolated nucleocapsids. Virus Res. 7, 131-149. 

Laurent, S., Vautherot, J. F., Madelaine, M. F., Le Gall, G., and Rasschaert, D. (1994). Recombinant rabbit hemorrhagic disease virus capsid protein expressed in baculovirus self assembles into virus like particles and induces protection./. Virol. 68, 6794-6798. 

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... 

Figure 10.17. Structure of rhino virus capsid protein VPl showing the bound conformation of antiviral isoxazole compounds (78) tdisoxaril, WIN-51711 panel a, top], (79)tWIN-54954 panel b, middle], and (80) [pleconaril, WIN-63843 panel c, bottom]. The PDB codes for the X-ray structural model coordinates used to create these views are IPIV (for 78), 2HWE (for 79), and 1C8M (for 80). On the left side of each panel, the inhibitors are shown as van der Waals surfaces, and the protein as a ribbon diagram. On the right side, the structures of the inhibitor alone are shown, from the same view, as ball and stick representations. See color insert.

YPMa is structurally most similar to virus capsid proteins and members of the TNF superfamily (table 1). However, there is no apparent amino acid sequence basis for the observed structural similarities. Structure-based... 

Fig. 2. The YPMa trimer shown with trimeric structures of virus capsid proteins and members of the TNF superfamily highlights the diversity of trimerization of jelly roll folds. Only C atoms of the polypeptide chains are shown. Virus trimers were extracted from the Viper database of virus structures (http //viperdb.scripps.edu/) [64], SPMV = Satellite pan-icum mosaic virus STMV = satellite tobacco mosaic virus. Figures 1 and 2 were created using Swiss-PdbViewer [65],... 

The structural similarity of YPM with virus capsid proteins and TNF superfamily members raises the possibility of an evolutionary relationship between these proteins. As discussed above, some staphylococcal and streptococcal superantigens are encoded by bacteriophages however, these superantigens are not structurally related to any known virus proteins. While no viral superantigens have been structurally characterized, the observed similarity of YPM with virus capsid proteins suggests a potential evolutionary link between viral and bacterial superantigens. 

Aoki N, Mori M, Kato K, et al. Antibody against synthetic multiple antigen peptides (MAP) of JG virus capsid protein (VPl) without cross reaction to BK virus a diagnostic tool fot progressive multifocal leukoencephalopathy. Neurosci Lett. 1996 205 111-114. 

The heat-labile toxin B subunit of E. coli (LTB) [398], hepatitis B surface antigen [404], respiratory syncytial virus F protein [258], measles virus hemagglutinin [180], and Norwalk virus capsid protein [240, 405, 406] have each been successfully expressed in plants and delivered orally in animals or humans to determine their im-munoprophylactic activity. The first account of a human clinical trial of oral vaccine based on an E. coli enterotoxin as... 

The variation measured by these tests is expressed on the virus capsid proteins which are coded for by the 30 to 40 6 of the virus BRA at the 5 iid (28). It is not known, however, vdiether variation is limited to this region of the genome. e have been studying the biochemical basis for variation by analysing the ERA and primary products of several isolates of the virus. 

Thus, the role of sialic acid in JC virus infection has been firmly established. Correspondingly, a linear sialylated pentasaccharide with the sequence NeuAc-a2,6-Gal-pl,4-GlcNAc-(31,3-Gal-(31,4-Glc present on host glycoproteins and glycolipids has been characterized as a specific JC virus recognition motif The crystal structure of the major JC virus capsid protein... 

Strand which then returns via two hairpin connections to the strand adjacent to the first. This feature contains a handedness that is only observed in one sense as shown in Fig. 13a. Connection of two of these features gives rise to an eight stranded y3-barrel however, Greek Key motifs are utilized in many ways to form closed structures. An alternative way of forming a closed barrel is found in proteins that exhibit a jelly roll topology (Fig. 13b). This is an abundant motif that is commonly found in virus capsid proteins. 

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