Disease relevance of Morbillivirus

• Markedly different fusion specificity was observed for another morbillivirus, canine distemper virus (CDV): recombinant CDV glycoproteins promoted fusion with primate and nonprimate cells independently of CD46 [1].
• A vaccine strain of peste des petits ruminants virus caused slight downregulation of CD46 in infected Vero cells, while wild-type and vaccine strains of canine distemper virus and a wild-type strain of dolphin morbillivirus failed to downregulate CD46 [2].
• Measles virus (MV) is the type species of the Morbillivirus genus and its RNA-dependent RNA polymerase complex is comprised of two viral polypeptides, the large (L) and the phospho- (P) proteins [3].
• The individual Morbillivirus glycans have similar functional properties: the glycan at position 68 is essential for protein transport, and those at positions 36 and 75 modulate fusion (numbering according to the Newcastle disease virus [NDV] F protein sequence) [4].
• RESULTS: Canine lymphoid cell lines and neoplastic B and T lymphocytes collected from dogs with spontaneous lymphoma expressed the Morbillivirus receptor CD150 mRNA [5].

High impact information on Morbillivirus

• In an in vivo replication/transcription system using a synthetic minigenome of RPV, we show that multimerization is essential for P protein function(s), and the multimerization domain is highly conserved between two morbilliviruses namely RPV and peste de petits ruminants virus [6].
• Rational attenuation of a morbillivirus by modulating the activity of the RNA-dependent RNA polymerase [7].
• To identify residues on the attachment protein hemagglutinin (H) essential for fusion support through either receptor, we devised a strategy based on analysis of morbillivirus H-protein sequences, iterative cycles of mutant protein production followed by receptor-based functional assays, and a novel MV H three-dimensional model [8].
• Based on the crystal structure of the NDV F protein, we then predicted the locations of the Morbillivirus glycans: the glycan at position 36 is located in the F protein head, and those at positions 68 and 75 are located near the neck-stalk interface [4].
• Immune responses to both the hemagglutinin (H) and the fusion (F) antigens of morbilliviruses play an important role in the prevention of infection, and only attenuated live vaccines have been shown to provide protective immunity against the group [9].

Chemical compound and disease context of Morbillivirus

• Viral glycoprotein (H) and nucleoprotein (N) expression in adherent blood monocytes and monocyte-derived macrophages was compared with the infection in Vero cells, in which a productive infection typical of morbilliviruses is obtained [10].
• Overall, the NP and in particular the F proteins of the morbilliviruses showed a high degree of epitopic homology; the P and M proteins showed a partial epitopic homology, with the greatest variation between the M proteins of CDV and MV; the H proteins showed a low degree of epitopic homology and then only between MV and RPV [11].
• As to their origin, it appears that the most likely source of the European seal morbillivirus (PDV-1) is the North Atlantic and Artic seal populations [12].
• As marine mammals are highly exposed to organochlorines, concentrations of PCBs, PCB MSFs, DDT, and DDE MSF were analyzed in blubber, lung, and uterus samples from harbor seal (Phoca vitulina) and striped dolphin (Stenella coeruleoalba) morbillivirus epizootic victims to investigate uterine and lung MSF accumulation [13].
• A monoclonal antibody with genus-specific reactivity for morbilliviruses was applied in an indirect immunoperoxidase method performed on formalin-fixed, paraffin-embedded tissue sections [14].

Biological context of Morbillivirus

• Six neutralizing epitopes were identified, at residues 474 (epitope A), 243 (B), 548 to 551 (D), 587 to 592 (E), 310 to 313 (G), and 383 to 387 (H), from the data on the amino acid substitutions of hemagglutinin protein of MAb-resistant mutants and the reactivities of MAbs against RPV-H to the other morbilliviruses [15].
• Although the HeV N protein had a slightly higher amino acid sequence identity to those of the genus Morbillivirus than to those of other Paramyxovirinae genera, the level of identity was much lower than that observed within the morbilliviruses [16].
• The nucleotide sequence of the phosphoprotein (P) gene of a dolphin morbillivirus (DMV) isolate was determined [17].
• Plasmid DNA containing a virus-specific insert, representing greater than 98% of the gene derived from the P-protein mRNA of canine distemper virus, showed significant cross-hybridisation with all the other members of the morbillivirus group [18].
• We have identified a "universal" morbillivirus primer set, based on highly conserved regions of the morbillivirus phosphoprotein (P) gene and used this to amplify a region surrounding the RNA editing site from all known members of the group [19].

Anatomical context of Morbillivirus

• Activated mouse T-cells synthesize MHC class II, process, and present morbillivirus nucleocapsid protein to primed T-cells [20].

Gene context of Morbillivirus

• In these three morbilliviruses, all strains examined were shown to use SLAMs of their respective host species, and laboratory strains passaged on SLAM-negative cells were found to use, besides SLAM, alternative receptors, such as human CD46 for the Edmonston strain of MV [21].
• As with other morbilliviruses, the phosphoprotein (P) gene of PDV was found to be located after the 5' end of the N gene and before the 3' end of the matrix protein gene [22].
• When the DMV N gene coding region was compared with the corresponding sequences of other morbilliviruses a distant evolutionary relationship between these viruses and DMV was apparent [23].
• This sequence, which is conserved in the N proteins of morbilliviruses, conforms well to the predicted algorithm for some of the most common BoLA CTL antigenic peptides [24].
• The morbillivirus receptor SLAM (CD150) [21].

Analytical, diagnostic and therapeutic context of Morbillivirus

• Recently an epizootic, reported to be due to a morbillivirus infection, affected the lion population of the Tanzanian Serengeti National Park. A morbillivirus phosphoprotein (P) gene fragment was amplified by PCR from tissue samples of several affected lions [25].

References