Disease relevance of NP

• Comparison of the amino acid sequences of the translation products with those of two Lassa virus strains showed considerable conservation, with 74 and 80% identity for the two glycoproteins G1 and G2, and 74% identity for the N protein [1].
• Conversely, the CH-specific antisera reacted with the nucleocapsid, GP2, and GPC proteins of LCMV [2].
• These antigens had the same electrophoretic mobilities on sodium dodecyl sulfate-polyacrylamide gels as did the nucleocapsid, GP2, and GPC proteins of lymphocytic choriomeningitis virus (LCMV) [2].
• Triton X-114 extraction and dimethyl suberimidate-HCl crosslinking indicate that the p11 Z protein is a hydrophobic protein associated with the nucleocapsid of the virion core [3].
• The Lister strain of vaccinia virus was used to construct a recombinant that expressed the nucleocapsid gene of Lassa virus [4].

High impact information on NP

• Identification of Lassa fever virus infection with recombinant nucleocapsid protein antigen [5].
• NP and L proteins of lymphocytic choriomeningitis virus (LCMV) are sufficient for efficient transcription and replication of LCMV genomic RNA analogs [6].
• A significant number (33%) of adult DT mice survived intracerebral infection with LCMV, suggesting that virus-induced immunopathology in the central nervous system can be diminished by combined expression of the transgenes whereas no protective effect was conferred on singly transgenic mice, expressing NP or GP alone [7].
• The genes encoding the VEE structural proteins were replaced with the influenza virus hemagglutinin (HA) or the Lassa virus nucleocapsid (N) gene, and upon transfection into eukaryotic cells by electroporation, these replicon RNAs directed the efficient, high-level synthesis of the HA or N proteins [8].
• Subcutaneous immunization of BALB/c mice with VRP expressing the influenza HA or Lassa virus N gene (HA-VRP or N-VRP, respectively) induced antibody responses to the expressed protein [8].

Biological context of NP

• The putative dibasic site of GPC cleavage (R-R) was conserved, as were the potential N-linked glycosylation sites [1].
• Molecular cloning of Lassa virus RNA: nucleotide sequence and expression of the nucleocapsid protein gene [9].
• Specific phosphorylation of N protein was reconfirmed in the purified nucleocapsid fraction and both phosphoserine and phosphothreonine found to be the phosphorylated products of the kinase reaction [10].
• The coding region of the gene for the nucleocapsid protein of Lassa virus has been inserted into the genome of Autographa californica nuclear polyhedrosis virus (AcNPV) using the transfer vector pAcYM1, so that expression of the foreign DNA is under the control of the promoter of the AcNPV polyhedrin gene [11].
• In this study, nucleocapsid protein gene sequence data were obtained for all currently known arenaviruses and used to estimate, for the first time, a phylogeny of the entire virus family [12].

Anatomical context of NP

• Fractionated RNAs were translated in rabbit reticulocyte lysates, and translation products were precipitated with monoclonal antibodies to the nucleocapsid protein of Lassa virus [13].

Associations of NP with chemical compounds

• The last-mentioned glycoprotein also appears to be complexed with p63, the main protein component of the nucleocapsid, and this in turn was found to be spatially associated with p200 [14].

Analytical, diagnostic and therapeutic context of NP

• The immunoperoxidase technique using monoclonal antibodies showed that persistently infected neurons primarily expressed the nucleocapsid protein antigens of LCMV [15].

References