Disease relevance of NP

• Marked differences in the apparent Mrs of the HN, NP and F proteins of simian virus 5 (SV5) and parainfluenza virus type 2 (PF-2) were revealed by SDS-PAGE [1].
• These antibodies had specificities for the HN, NP and P proteins and together with 54 MAbs to SV5 were tested for their ability to react with SV5, PF-2, PF-3, mumps and measles virus proteins [1].
• Six other Sendai virus monoclonal antibodies directed against four different epitopes of the HN protein and one directed against the NP protein cross-reacted with mumps virus [2].
• A recombinant baculovirus expressing the nucleocapsid gene (NP) of Newcastle disease virus (NDV), a member of the genus Rubulavirus, has been generated and shown to express the native protein to high levels in insect cells [3].
• Significant differences in nucleocapsid morphology within the Paramyxoviridae [4].

High impact information on NP

• Two regions of mumps virus were amplified: the nucleocapsid gene and the polymerase-associated protein gene [5].
• Variations were found in four, three, and three different antigenic sites of the NP, P, and HN proteins, respectively [6].
• A recombinant expression plasmid was designed to produce antisense oligonucleotides targeted to the 5' end of the MV nucleocapsid protein mRNA [7].
• The epitopes recognized by 41 monoclonal antibodies directed against the nucleocapsid protein (NP) of human parainfluenza virus type 2 (hPIV-2) were mapped on the primary structure of the hPIV-2 NP protein by testing their reactivities with deletion mutants [8].
• Therefore, we conclude that the P protein acts as a chaperone, preventing uncontrolled encapsidation of non-viral RNA by NP protein [3].

Chemical compound and disease context of NP

• In contrast to the NP protein of the rubulavirus human parainfluenza virus 2, the NDV protein has been demonstrated by electron microscopy and caesium chloride gradient analysis to be capable of self-assembly in vivo to form nucleocapsid-like structures in the absence of other NDV proteins [3].
• Patients with antibody rises in parainfluenza or mumps virus antibodies were studied for cross-reactions by CF, hemagglutination inhibition (HAI), and EIA using purified viral envelope glycoprotein and nucleocapsid preparations [9].
• Rabbit antibodies against the invariant chain peptide also reacted with nucleocapsid molecules in formaldehyde-fixed mumps virus-infected cells, and antibodies against the nucleocapsid peptide reacted with invariant chains expressed in methanol-fixed cells [10].

Biological context of NP

• Sequence analyses of the 3' genome end and NP gene of human parainfluenza type 2 virus: sequence variation of the gene-starting signal and the conserved 3' end [11].
• A primer extension analysis elucidated the major NP mRNA initiation site with the sequence UCUAAGCC, which showed a moderate homology with the gene-starting consensus sequences of other paramyxoviruses [11].
• We cloned and determined the nucleotide sequences of cDNAs against nucleocapsid protein (NP) mRNA and the genomic RNA of human parainfluenza type 2 virus (PIV-2) [11].
• Interaction between nucleocapsid protein (NP) and phosphoprotein (P) of human parainfluenza virus type 2: one of the two NP binding sites on P is essential for granule formation [12].
• cDNA clones of the mumps virus N and P messenger RNAs were isolated from an infected cell cDNA library [13].

Anatomical context of NP

• Of 30 hybridoma clones against PIV-4B, 13 clones were found to produce antibodies against the NP protein, 7 against the HN protein, and 10 against the F protein [14].
• When using the MAb against the NP protein, nucleocapsid organization was the most prominent feature and resulted in the formation of cytoplasmic inclusion bodies visible by light and electron microscopy [15].
• To study the interaction between NP and P proteins, we established HeLa cell lines that constitutively expressed the NP and/or P proteins of human parainfluenza virus type 2 (hPIV-2) [12].
• Ribozyme-mediated decrease in mumps virus nucleocapsid mRNA level and progeny in infected vero cells [16].
• The proliferative T lymphocyte responses to two different mumps antigen preparations, S (nucleocapsid) and V (viral envelope), were characterized [17].

Associations of NP with chemical compounds

• The recombinant nucleocapsid protein was purified by cesium chloride ultracentrifugation of yeast lysates [18].

Analytical, diagnostic and therapeutic context of NP

• CsCl density gradient centrifugation indicated that almost all of the NP protein in the cells had assembled into nucleocapsid-like structures [19].
• In the HN and NP components, RIPA revealed variations in three and seven determinants respectively [20].
• In addition, cells co-expressing NP and P proteins with N-terminal deletions showed immunofluorescence staining patterns (granular pattern) similar to those found in hPIV-2-infected cells [12].
• Co-immunoprecipitation assays revealed that the NP and P proteins can form complexes in HeLa cells expressing both proteins (HeLa-NP+P cells) and in mixed cell lysates of HeLa-NP and HeLa-P cells [12].
• In situ hybridization carried out with a 3H-labeled DNA probe, specific for the measles nucleocapsid protein, detects measles virus nucleotide sequences in the nuclei and cytoplasm of pagetic osteoclasts, confirming ultrastructural and immunocytologic findings [21].

References