Disease relevance of NP

• The complete VP1 protein of EV71 was truncated into six segments and fused to the C-terminal ends of full-length nucleocapsid protein (NPfl) and truncated NP (NPt; lacks 20% amino acid residues from its C-terminal end) of newcastle disease virus (NDV) [1].
• In the present study, the performances of conventional purification methods, packed bed adsorption (PBA), and expanded bed adsorption (EBA) for the purification of the nucleocapsid protein (NP) of Newcastle disease virus (NDV) from Escherichia coli homogenates were evaluated [2].
• Several electrophoretic variants of the nucleocapsid protein that were probably created by intrachain disulfide bonding were also isolated from virions under nonreducing conditions [3].
• When analyzed by polyacryl-amide gel electrophoresis, the nucleocapsids consisted of the nucleocapsid protein, a minor protein of 53,000 molecular weight, and the large L protein [4].
• Another measure of specificity was the fact that 400 ng of purified nucleocapsid protein from simian virus 5, Newcastle disease virus or canine distemper virus did not react in the assay [5].

High impact information on NP

• The nucleocapsid-associated polypeptides most likely to be involved in RNA synthesis are located at the extreme ends of the genome: NP and P are promoter proximal genes, and L is the most distal gene [6].
• Under these conditions, infected cells synthesized proteins which comigrated on polyacrylamide gels with the viral L protein, nucleocapsid protein, membrane protein, and a polypeptide with a molecular weight of 55,000 (P55) [7].
• Newcastle disease virus nucleocapsid protein: self-assembly and length-determination domains [8].
• The CAT gene was under the control of NDV transcriptional start and stop signals and was inserted immediately before the open reading frame of the viral 3'-proximal nucleocapsid protein gene [9].
• Monoclonal antibodies to the haemagglutinin-neuraminidase (HN), fusion (F), polymerase and nucleocapsid polypeptides of Newcastle disease virus were prepared [10].

Chemical compound and disease context of NP

• The nucleotide sequences of the nucleocapsid protein (NP) gene, the intergenic regions in the nucleocapsid protein (NP)-phosphoprotein (P), P-matrix protein (M) and M-fusion glycoprotein gene junctions and the trailer region of a virulent Newcastle disease virus (NDV) strain Beaudette C were determined [11].

Biological context of NP

• A phylogenetic tree construct based on the nucleotide sequence of the complete NP gene revealed that the old (prior to 1970s) and the new (after 1980s) isolates could be classified into two major different groups, i.e., a group comprising virulent strains, and another group composed of avirulent strains [12].
• By deduced amino acid sequence comparison, the N-terminal region (from 1 to 401 residues) of the NP protein was found to be highly conserved, while the C-terminal region was highly variable among the NDV isolates [12].
• An in vitro protein binding assay was used to investigate the regions on NP protein that interact with the P protein of Newcastle disease virus (NDV) [13].
• The nucleocapsid (NP) and phospho-(P) proteins of paramyxoviruses are involved in transcription and replication of the viral genome [13].
• Analysis of DTBP-treated NDV revealed crosslinking between a nucleocapsid protein, VP3, and an externally displayed glycoprotein, VP1, possessing hemagglutination and neuraminidase activities [14].

Anatomical context of NP

• Truncated NP mutants were first immobilised on a solid phase and then interacted with radio-labelled [(35)S]-P protein synthesised in rabbit reticulocyte [13].

Associations of NP with chemical compounds

• The conventional methods for the recovery of NP proteins involved multiple steps, such as centrifugation, precipitation, dialysis, and sucrose gradient ultracentrifugation [2].
• The results indicated that homodimers of glycoprotein, nucleocapsid protein and M protein were generated under the condition of the most gentle cross-linking employed [15].

Physical interactions of NP

• Regions on nucleocapsid protein of Newcastle disease virus that interact with its phosphoprotein [13].

Other interactions of NP

• With the aid of these mAbs, the structural proteins of BaV were determined, namely, p52, gp74, gp63, and gp51 were identified as the NP, HN, F0, and F1 proteins, respectively [16].

Analytical, diagnostic and therapeutic context of NP

• The transcriptive complex, recovered at a density of 1.275 g/cm3, appeared as a nucleocapsid structure by electron microscopy [4].
• Baculovirus-expressed N proteins were used as antigen in an indirect enzyme-linked immunosorbent assay (ELISA) for detection of TCV-specific antibodies [17].
• A diagnostic immunoassay for Newcastle disease virus based on the nucleocapsid protein expressed by a recombinant baculovirus [18].

References