Disease relevance of RGSVs5gp2

• These results suggest that dimerization and encapsidation of genome length RSV RNA might be linked in the course of virion formation since they appear to be under the control of the same cis elements, E and DLS, and the trans-acting factor nucleocapsid protein NCp12 [1].
• Solution Structure of the Rous Sarcoma Virus Nucleocapsid Protein: muPsi RNA Packaging Signal Complex [2].
• Since some retroviruses only have one such motif, we have investigated the significance of the two distinct Cys-His motifs of RSV NC [3].
• Integration with RSV RT alphabeta could be stimulated in the presence of human immunodeficiency virus type 1 nucleocapsid protein or HMG-I(Y) [4].
• To determine whether specific packaging of viral RNA is mediated by NC in vivo, we have constructed RSV mutants carrying sequences of Moloney murine leukemia virus (MoMuLV) [5].

High impact information on RGSVs5gp2

• Using this model RSV RNA was shown to form dimeric molecules and this dimerization process was greatly activated by nucleocapsid protein (NCp12) of RSV [1].
• We now report the solution structure of the NC:muPsi complex, determined using NMR data obtained for samples containing ((13)C,(15)N)-labeled NC and (2)H-enriched, nucleotide-specifically protonated RNAs [2].
• NC does not bind with significant affinity to truncated forms of muPsi, consistent with earlier packaging and mutagenesis studies [6].
• The importance of the nucleocapsid (NC) domain in membrane targeting was also determined, and, importantly, deletion of the NC sequence prevented plasma membrane localization by wild-type Gag but not by Super M Gag [7].
• In this paper we show that the basic residues of nucleocapsid protein NCp10 of Moloney murine leukemia virus (MoMuLV), but not the zinc finger, are necessary for minus strand transfer [8].

Biological context of RGSVs5gp2

• Surprisingly, the full-deletion mutant showed a strong block in virus release, suggesting that NC is involved in virus assembly [5].
• Either the NC coding region alone, the psi RNA packaging sequence, or both the NC and psi sequences of MoMuLV were substituted for the corresponding regions of a full-length RSV clone to yield chimeric plasmid pAPrcMNC, pAPrc psi M, or pAPrcM psi M, respectively [5].
• However, it has not been possible to demonstrate, in vivo or in vitro, specific binding of viral RNA sequences by NC [5].
• The analysis of the phenotype of virus NC mutants with precise rearrangements or duplications of the motifs highlights the following features [3].
• The mRNA transcripts corresponding to open reading frames for the non-structural protein (NS4) and nucleocapsid protein (N), which are encoded on virus-sense (v) RNA 4 and virus-complementary sense (vc) RNA 3, respectively, were recovered from polysomes of RSV-infected wheat leaves, and their 5' termini were analysed [9].

Anatomical context of RGSVs5gp2

• Pagetic osteoclasts express respiratory syncytial viral (RSV) and measles viral (MV) nucleocapsid antigens [10].
• Inhibition of respiratory syncytial virus in cultured cells by nucleocapsid gene targeted deoxyribozyme (DNAzyme) [11].

Associations of RGSVs5gp2 with chemical compounds

• MAbs to an irrelevant antigen (pneumococcal polysaccharide) and to the nucleocapsid of RSV did not enhance infection [12].
• The recombinant N protein was purified from infected-cell extracts by sucrose gradient centrifugation and used in the ELISA for the detection of antibodies to various RSV strains [13].
• Two monoclonal antibodies, one each directed against a surface glycoprotein and the nucleocapsid protein, were then compared, singly and combined, with a polyclonal antiserum as diagnostic reagents in 209 consecutive samples submitted to our diagnostic laboratory [14].
• The introduction of two proline residues to disrupt the predicted alpha-helical domain in this region dramatically reduced the ability of the mutant P protein to interact with the N protein [15].

Analytical, diagnostic and therapeutic context of RGSVs5gp2

• Site-directed mutagenesis has shown that the nucleocapsid (NC) protein of Rous sarcoma virus (RSV) is required for packaging and dimerization of viral RNA [5].
• Our results indicate that the ELISA with the baculovirus-expressed N protein as an antigen is an efficient, sensitive, and specific method for detecting serum antibodies to RSV [13].
• When recombinant N was purified on CsCl gradients, two types of structure, both with densities indicating that they contained RNA, could be visualised by negative-stain electron microscopy [16].
• This protein was indistinguishable from the authentic bovine respiratory syncytial virus (BRSV) N protein by SDS-gel electrophoresis and immunoprecipitation with anti-BRSV serum [17].
• Purified viral nucleocapsid (RNP) isolated from virus-infected cells was shown to support transcription of all 10 genes encoded by the virus as determined by Northern blot hybridization [18].

References