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].

References