The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

CP  -  capsid protein

Cucumber mosaic virus

Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of CP

  • The capsid protein (CP) of Cucumber mosaic virus (CMV) is required for cell-to-cell movement, mediated by the 3a movement protein (MP) [1].
  • The 3a movement protein (MP) of a plant virus, Cucumber mosaic virus (CMV), forms ribonucleoprotein (RNP) complexes with viral RNA, capable of trafficking from cell-to-cell throughout the infected plant only in the presence of the CMV capsid protein (CP) [2].
  • Moreover, while the CP is necessary for cell-to-cell movement, the ability to form virions is not a prerequisite for cell-to-cell movement [3].
  • The CyRSV CP was expressed only in the leaves which were inoculated with DI-3CPWt plus CP-less mutant helper virus (delta ABgII) [4].
  • Dissecting human cytomegalovirus gene function and capsid maturation by ribozyme targeting and electron cryomicroscopy [5].

High impact information on CP

  • CMV capsid protein loop mutants with single-amino-acid substitutions are unable to systemically infect squash, but they revert to a wild-type phenotype in the presence of an additional, specific single-site substitution [6].
  • Cleavage is essential for capsid maturation and production of infectious virus, but the role of phosphorylation is undetermined [7].
  • Especially appealing is the ability of the CMV genome to persist in hematopoietic progenitor cells and the packaging capacity of the viral capsid that accommodates a DNA genome of 230 kbp [8].
  • Recombinant vaccinia virus encoding individual adenovirus proteins showed that the T cell response to the adenovirus was directed mainly against the capsid protein hexon [9].
  • The relevance of these findings to early steps in capsid assembly, the mechanism of MCP nuclear transport, and the possible cytoplasmic formation of protocapsomeric substructures is discussed [10].

Chemical compound and disease context of CP

  • Herpesviruses encode an essential serine proteinase called assemblin that is responsible for cleaving the precursor assembly protein during the process of capsid formation [11].

Biological context of CP

  • In the present study, the nucleotide sequences of the 3a and CP genes of SSV were determined, and the data were used to classify seven SSV isolates among known Cucumber mosaic virus (CMV) strains [12].
  • We obtained mutants containing mutations in the two open reading frames in CMV RNA3 encoding the 3a protein and the capsid protein (CP), both of which are necessary for cell-to-cell movement of CMV [13].
  • Chimaeric DI RNA carrying a heterologous CP gene (DI-3HCPtav) was able to replicate and express the inserted TAV CP in the presence of a wild-type (wt) helper genome [4].
  • Both constructs, which were stable and active for gene expression, carried the inserted CP genes in the same position, between the A and B blocks of DI-3 RNA [4].
  • Post-translational glycosylation or phosphorylation were also ruled out as contributing factors to the observed anomalous electrophoretic mobility because the products of in vitro translation of cucumovirus RNA 4 and in vivo bacterial expression of the cloned CP gene co-migrated with authentic cucumovirus CPs [14].

Anatomical context of CP

  • Encapsidation assays in N. benthamiana protoplasts revealed that CMV CP expressed from chimeric BMV RNA3 was capable of packaging heterologous BMV RNA, however, at a lower efficiency than parental BMV CP [15].
  • Human cytomegalovirus (CMV) infects cells by sequential processes involving attachment, fusion with the cell membrane, and penetration of the capsid [16].
  • A cDNA encoding the 37-kilodalton (kDa) capsid assembly protein of cytomegalovirus (CMV) strain Colburn was isolated from a lambda gt11 library constructed from CMV Colburn-infected human fibroblast RNA [17].

Associations of CP with chemical compounds

  • Segments of three nucleotides of partially disordered RNA interact with the capsid, primarily through arginine residues, at interfaces between A and B subunits [18].
  • Favorable binding to the swollen form suggests that Ca(2+) ions can induce the capsid contraction and stabilize the native form [19].

Analytical, diagnostic and therapeutic context of CP

  • A productive CMV cycle in the CR-10/NIT lymphoblasts was demonstrated by fluorescent antibody staining (IF) using a monoclonal antibody (MAb) to the 150-kDa major capsid protein, by infectivity assays and by electron microscopy (EM) [20].
  • Western-blot analysis of the in vitro translation products revealed that the 17,500 Mr protein had the same electrophoretic mobility as the authentic capsid protein; it was also antigenically related to the capsid protein, but the 6800 Mr protein was not [21].
  • Immunoperoxidase staining for papilloma virus capsid antigen could be combined with DNA in situ hybridization with HPV-6/11 DNA [22].
  • Anti-CMV IgG and IgM antibody titres and anti-EBV capsid antigen IgG, IgA, IgM, and EBV nuclear antigen and EBV early antigen IgG titres were determined by enzyme immunoassay [23].
  • These findings suggest the entry of HCMV into lymphoma cells with positive PCR amplification of DNA encoding an early structural protein, and replication from the presence of late structures of virus, electron-dense core and capsid [24].


  1. The C-terminal 33 amino acids of the cucumber mosaic virus 3a protein affect virus movement, RNA binding and inhibition of infection and translation. Kim, S.H., Kalinina, N.O., Andreev, I., Ryabov, E.V., Fitzgerald, A.G., Taliansky, M.E., Palukaitis, P. J. Gen. Virol. (2004) [Pubmed]
  2. Molecular interactions between a plant virus movement protein and RNA: force spectroscopy investigation. Andreev, I.A., Hyon Kim, S., Kalinina, N.O., Rakitina, D.V., Fitzgerald, A.G., Palukaitis, P., Taliansky, M.E. J. Mol. Biol. (2004) [Pubmed]
  3. Characterization of cucumber mosaic virus. V. Cell-to-cell movement requires capsid protein but not virions. Kaplan, I.B., Zhang, L., Palukaitis, P. Virology (1998) [Pubmed]
  4. Expression of homologous and heterologous viral coat protein-encoding genes using recombinant DI RNA from cymbidium ringspot tombusvirus. Burgyán, J., Salánki, K., Dalmay, T., Russo, M. Gene (1994) [Pubmed]
  5. Dissecting human cytomegalovirus gene function and capsid maturation by ribozyme targeting and electron cryomicroscopy. Yu, X., Trang, P., Shah, S., Atanasov, I., Kim, Y.H., Bai, Y., Zhou, Z.H., Liu, F. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  6. Compensatory capsid protein mutations in cucumber mosaic virus confer systemic infectivity in squash (Cucurbita pepo). Thompson, J.R., Doun, S., Perry, K.L. J. Virol. (2006) [Pubmed]
  7. Assembly protein precursor (pUL80.5 homolog) of simian cytomegalovirus is phosphorylated at a glycogen synthase kinase 3 site and its downstream "priming" site: phosphorylation affects interactions of protein with itself and with major capsid protein. Casaday, R.J., Bailey, J.R., Kalb, S.R., Brignole, E.J., Loveland, A.N., Cotter, R.J., Gibson, W. J. Virol. (2004) [Pubmed]
  8. Construction of a cytomegalovirus-based amplicon: a vector with a unique transfer capacity. Borst, E.M., Messerle, M. Hum. Gene Ther. (2003) [Pubmed]
  9. Adenovirally transduced dendritic cells induce bispecific cytotoxic T lymphocyte responses against adenovirus and cytomegalovirus pp65 or against adenovirus and Epstein-Barr virus EBNA3C protein: a novel approach for immunotherapy. Hamel, Y., Blake, N., Gabrielsson, S., Haigh, T., Jooss, K., Martinache, C., Caillat-Zucman, S., Rickinson, A.B., Hacein-Bey, S., Fischer, A., Cavazzana-Calvo, M. Hum. Gene Ther. (2002) [Pubmed]
  10. Cytomegalovirus assembly protein precursor and proteinase precursor contain two nuclear localization signals that mediate their own nuclear translocation and that of the major capsid protein. Plafker, S.M., Gibson, W. J. Virol. (1998) [Pubmed]
  11. Independently cloned halves of cytomegalovirus assemblin, An and Ac, can restore proteolytic activity to assemblin mutants by intermolecular complementation. Hall, M.R., Gibson, W. J. Virol. (1997) [Pubmed]
  12. Adaptation of Cucumber mosaic virus soybean strains (SSVs) to cultivated and wild soybeans. Hong, J.S., Masuta, C., Nakano, M., Abe, J., Uyeda, I. Theor. Appl. Genet. (2003) [Pubmed]
  13. Role of cucumovirus capsid protein in long-distance movement within the infected plant. Taliansky, M.E., García-Arenal, F. J. Virol. (1995) [Pubmed]
  14. The conserved, hydrophilic and arginine-rich N-terminal domain of cucumovirus coat proteins contributes to their anomalous electrophoretic mobilities in sodium dodecylsulfate-polyacrylamide gels. Hu, C.C., Ghabrial, S.A. J. Virol. Methods (1995) [Pubmed]
  15. Molecular studies on bromovirus capsid protein. Osman, F., Choi, Y.G., Grantham, G.L., Rao, A.L. Virology (1998) [Pubmed]
  16. Anti-idiotype antibodies that mimic gp86 of human cytomegalovirus inhibit viral fusion but not attachment. Keay, S., Baldwin, B. J. Virol. (1991) [Pubmed]
  17. Primate cytomegalovirus assembly protein: genome location and nucleotide sequence. Robson, L., Gibson, W. J. Virol. (1989) [Pubmed]
  18. The structure of tomato aspermy virus by X-ray crystallography. Lucas, R.W., Larson, S.B., Canady, M.A., McPherson, A. J. Struct. Biol. (2002) [Pubmed]
  19. Electrostatic properties of cowpea chlorotic mottle virus and cucumber mosaic virus capsids. Konecny, R., Trylska, J., Tama, F., Zhang, D., Baker, N.A., Brooks, C.L., McCammon, J.A. Biopolymers (2006) [Pubmed]
  20. Cytomegalovirus enhances lysis of HIV-infected T lymphoblasts. Casareale, D., Fiala, M., Chang, C.M., Cone, L.A., Mocarski, E.S. Int. J. Cancer (1989) [Pubmed]
  21. Nucleotide sequence and translation of satellite tobacco mosaic virus RNA. Mirkov, T.E., Mathews, D.M., Du Plessis, D.H., Dodds, J.A. Virology (1989) [Pubmed]
  22. Combined immuno- and non-radioactive hybridocytochemistry on cells and tissue sections: influence of fixation, enzyme pre-treatment, and choice of chromogen on detection of antigen and DNA sequences. Mullink, H., Walboomers, J.M., Tadema, T.M., Jansen, D.J., Meijer, C.J. J. Histochem. Cytochem. (1989) [Pubmed]
  23. Reactivation of human herpesvirus (HHV) family members other than HHV-6 in drug-induced hypersensitivity syndrome. Seishima, M., Yamanaka, S., Fujisawa, T., Tohyama, M., Hashimoto, K. Br. J. Dermatol. (2006) [Pubmed]
  24. Detection of human cytomegalovirus in pleural fluid of lymphoblastic lymphoma T-cell type. Hirose, Y., Takeshita, S., Konda, S., Takiguchi, T. Int. J. Hematol. (1994) [Pubmed]
WikiGenes - Universities