Disease relevance of Rinderpest

• Long-term sterilizing immunity to rinderpest in cattle vaccinated with a recombinant vaccinia virus expressing high levels of the fusion and hemagglutinin glycoproteins [1].
• Monoclonal antibodies (mAbs) against secreted hemagglutinin (H) protein of rinderpest virus (RPV) expressed by a recombinant baculovirus were generated to characterize the antigenic sites on H protein and regions of functional significance [2].
• Cloning and sequence analysis of the matrix (M) protein gene of rinderpest virus and evidence for another bovine morbillivirus [3].
• Monospecific and monoclonal antibodies against measles virus and canine distemper virus hemagglutinin, fusion protein, nucleocapsid protein, and phosphoproteins confirmed the identity of the corresponding rinderpest virus-specific polypeptides [4].
• The homology comparisons in P amino acid sequences between rinderpest and measles, between rinderpest and canine distemper, and between rinderpest and phocid distemper viruses are 60, 44, and 46%, respectively [5].

High impact information on Rinderpest

• Phosphoprotein of the rinderpest virus forms a tetramer through a coiled coil region important for biological function. A structural insight [6].
• We report here the characterization of oligomeric P protein of rinderpest virus (RPV) and provide a structural basis for its multimerization [6].
• We previously demonstrated that the rinderpest virus (RPV) hemagglutinin (H) protein plays an important role in determining host range but that other viral proteins are clearly required for full RPV pathogenicity to be manifest in different species [7].
• In this study we show that CD46 is also downregulated to the same extent by wild-type, vaccine, and laboratory-passaged strains of rinderpest virus (RPV), although CD46 did not appear to be the receptor for RPV [8].
• Administration of acetylsalicylic acid or mefenamic acid during experimental infection of rabbits with a rabbit-adapted strain of rinderpest virus did not prevent initiation of the febrile response but significantly reduced the duration of fever [9].

Chemical compound and disease context of Rinderpest

• An indirect ELISA was used successfully to evaluate the status of cattle following the Pan African Rinderpest Campaign [10].
• Preparation and characterization of monoclonal antibodies to nucleocapsid protein N and H glycoprotein of rinderpest virus [11].
• Inhibition of replication of rinderpest virus by 5-fluorouracil [12].
• Three new potential sequence motifs with homology to the alpha-subunit of the polymerase-associated nucleocapsid phosphoprotein of rinderpest virus, the Bowman-Birk type of proteinase inhibitors, and the metallothionein superfamily of cysteine rich chelating proteins have been identified [13].
• Immunohistological localisation of rinderpest virus in formalin-fixed, paraffin-embedded tissues from experimentally infected cattle [14].

Biological context of Rinderpest

• Nucleotide sequence of cDNA to the rinderpest virus mRNA encoding the nucleocapsid protein [15].

Anatomical context of Rinderpest

• Mapping of B-cell epitopes of hemagglutinin protein of rinderpest virus [2].
• In the present work, we have shown that anti-idiotypic T cells are generated in mice after immunization with idiotypic T cell clone or polyclonal T cell specific for nucleocapsid protein of Rinderpest virus [16].
• Effect of ammonium chloride on multiplication of rinderpest virus in Vero cells [17].

Gene context of Rinderpest

• Domains of Rinderpest virus phosphoprotein involved in interaction with itself and the nucleocapsid protein [18].
• The yeast two-hybrid system was used to identify domains involved in specific in vivo interactions between the Rinderpest virus (RPV) phosphoprotein (P) and nucleocapsid protein (N) [18].
• Sequencing and analysis of the nucleocapsid (N) and polymerase (L) genes and the terminal extragenic domains of the vaccine strain of rinderpest virus [19].
• A total of 24 monoclonal antibodies (MAbs) against the haemagglutinin (H) and the fusion protein (F) of rinderpest virus (RPV) were used to characterize their antigenic structure and biological properties, and to analyse natural variation in the envelope proteins of morbilliviruses [20].
• Cross-linking and circular dichroism analyses indicated that fragment X was oligomeric, with a high alpha-helical content, properties resembling those of the multimerization domain of Sendai and rinderpest virus P [21].

Analytical, diagnostic and therapeutic context of Rinderpest

• Competitive enzyme-linked immunosorbent assay based on monoclonal antibody and recombinant hemagglutinin for serosurveillance of rinderpest virus [22].
• Cloning and expression of the nucleocapsid gene of virulent Kabete O strain of rinderpest virus in baculovirus: use in differential diagnosis between vaccinated and infected animals [23].
• Molecular cloning and sequence analysis of the rinderpest virus mRNA encoding the hemagglutinin protein [24].
• Simple and rapid dot-enzyme immunoassay for visual detection of rinderpest antibodies in bovine and caprine sera [25].

References