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PubMed1994

Nucleotide sequence comparisons of the fusion protein gene from virulent and attenuated strains of rinderpest virus.

We have cloned and sequenced the entire fusion (F) protein gene of the RBOK vaccine strain of rinderpest virus and the coding regions for the F genes of two mild field isolates of the virus from Africa. Analysis of the nucleotide and the predicted amino acid sequences showed that the vaccine virus was more than 99% identical in the protein coding region to the virulent Kabete O strain from which it was derived, whereas the field isolates differed by 10 to 12% from each other and from the vaccine strain. No changes were found in the F protein which could explain attenuation of the vaccine; however, each of the mild field isolates had amino acid changes in important functional areas which may be related to their attenuated phenotype.

Africa↗
PubMed1996

The genome sequence of the virulent Kabete 'O' strain of rinderpest virus: comparison with the derived vaccine.

We have compared the complete genome sequences of the vaccine strain of rinderpest virus and the virulent strain from which it was derived. Only 87 bases differed between the two genomes (0.55%). Possibly significant differences in amino acid sequence were found in the N, P, F, H and L proteins. A number of differences were also found in the leader region (3' end of the genome), whilst the trailer region appears to be more conserved. In addition, the length of the genome was found in both cases to be 15882, an exact multiple of six, fulfilling predictions made earlier based on work with Sendai and measles viruses.

Base Sequence↗
PubMed1997

Rinderpest virus isolates of different virulence vary in their capacity to infect bovine monocytes and macrophages.

Three isolates of rinderpest virus (RPV) with different in vivo virulence were able to infect and productively replicate in bovine monocytic cells. They differed in their kinetics of replication and the morphological changes induced in infected cultures. The highly virulent RPV-Saudi infected > 80% of cells within 6 days p.i. (m.o.i. = 0.1 TCID50 per cell). Under identical conditions, > 50% of cells were infected by the 'mild' (causes minimal mortality in vivo) isolate RPV-Egypt, whereas only 25% were infected by the avirulent RPV-RBOK. Infection by all three viruses produced infectious progeny, induced the formation of syncytia and stellate cells with long processes, and down-regulated MHC class II expression; there was no apparent effect on MHC class I nor LFA-1. RPV-Saudi was the most efficient at generating progeny virus and producing syncytia. While RPV-RBOK was the least efficient at inducing syncytia, RPV-Egypt was the least efficient for progeny virus production. In contrast, RPV-Egypt was particularly efficient at inducing stellate cell formation and down-regulating MHC class II expression. These results indicate a relationship between in vivo virulence and the characteristics of replication and induced morphological changes in monocytes/macrophages. The down-regulation of MHC class II expression would offer a means by which the virus could evade immune recognition. This would be particularly useful for the more cell-associated, but less efficient at maturing, RPV-Egypt.

Animals↗
PubMed1999

Expression in cattle of epitopes of a heterologous virus using a recombinant rinderpest virus.

We have investigated the bovine immune response to heterologous proteins expressed using a recombinant rinderpest virus (RPV). A new gene unit was created in a cDNA copy of the genome of the vaccine strain of RPV, and an open reading frame inserted that encodes the polymerase (3Dpol) and parts of the capsid protein VP1 from foot-and-mouth disease virus (FMDV). Infectious recombinant RPV was rescued and shown to express the FMDV-derived protein at good levels in infected cells. The rescued virus was only slightly more attenuated in tissue culture than the original virus. Cattle infected with this recombinant generated a normal immune response to RPV, and were protected from lethal challenge by that virus. Experimental animals showed a specific delayed-type hypersensitivity response to FMDV 3Dpol, similar to that seen in FMDV infection; however, no antibodies were detected recognizing either of the components of the FMDV-derived protein, nor was any proliferative response to these epitopes found in isolated peripheral blood lymphocytes from infected animals. No protection was seen against FMDV infection.

Animals↗
PubMed2001

Scanning mutagenesis identifies critical residues in the rinderpest virus genome promoter.

Short regions at the 3' and 5' ends of the genome of Rinderpest virus (RPV) contain signals that regulate transcription of the viral genome, known as the genome promoter and the (complement to the) antigenome promoter, respectively. An RPV minigenome construct carrying the CAT coding sequence was used as a reporter to investigate residues in the 3'-terminal region of the genome important for these functions. Single-base scanning mutagenesis showed that modifications to nucleotides 1, 3, 4, 10 and 19 of the RPV leader had an extremely inhibitory effect on transcription and/or encapsidation of the minigenome, with CAT expression reduced to 0-10% of control values. Changes in any of the other first 22 nucleotides reduced the efficiency of the minigenome to 20-80% of the wild-type control, with the exception of nucleotides 16, 17 and 20, where mutations did not affect CAT expression significantly. Mutagenesis in blocks identified critical residues in positions 23-26, but changes to leader residues 27-48 had no major effect on CAT expression. A region of about 16 nucleotides (49-65) located around the start of the nucleocapsid gene, including the intergenic triplet CTT, was identified as essential for minigenome function. Mutations further into the nucleocapsid gene (nt 66-89) had a moderate effect (CAT activity 20-60% of control), while at least one critical residue was found in positions 93-96. The importance of four highly conserved G residues at positions 79, 85, 91 and 97 was also investigated. G79 was found to be optimal, though not critical, while a purine was required at 85 and 91. Although G97 is conserved in morbilliviruses, all bases were equally effective at this position.

3' Untranslated Regions↗
PubMed2004

Cellular casein kinase II-mediated phosphorylation of rinderpest virus P protein is a prerequisite for its role in replication/transcription of the genome.

Phosphoprotein P of rinderpest virus (RPV), when expressed in E. coli, is present in the unphosphorylated form. Bacterially expressed P protein was phosphorylated by a eukaryotic cellular extract, and casein kinase II (CK II) was identified as the cellular kinase involved in phosphorylation. In vitro phosphorylation of P-deletion mutants identified the N terminus as a phosphorylation domain. In vivo phosphorylation of single or multiple serine mutants of P protein identified serine residues at 49, 88 and 151 as phospho-acceptor residues. The role of P protein phosphorylation in virus replication/transcription was evaluated using the RPV minigenome system and replication/transcription of a reporter gene in vivo. P protein phosphorylation was shown to be essential for in vivo replication/transcription since phosphorylation-null mutants do not support expression of a reporter gene. Transfection of increased amounts of phosphorylation-null mutant did not support minigenome replication/transcription in vivo.

Amino Acid Sequence↗
PubMed2005

Wild-type Rinderpest virus uses SLAM (CD150) as its receptor.

Rinderpest virus (RPV) is a morbillivirus, related closely to the human pathogen Measles virus (MV). Although cell culture-adapted strains of RPV can infect many kinds of cell from different hosts, one such strain has previously been shown to have a detectable preference for cells expressing the MV receptor CD150 (SLAM), a protein found only on certain types of activated T cells, B cells and dendritic cells. Here, it is shown that the wild-type, virulent parent of the most common vaccine strain of RPV requires CD150 as a receptor, whilst the cell culture-adapted vaccine strain has acquired the ability to use heparan sulphate as an alternative receptor.

Adaptation, Physiological↗
PubMed1990

Temporary breakdown of immunological tolerance to dsDNA and nucleohistone antigens in rabbits infected with rinderpest virus.

The rabbit-passaged L strain of rinderpest virus (RV) causes the transient induction of anti-nuclear antibodies (ANA) in rabbits. It has been shown by an indirect immunofluorescence test that the target antigens of these ANA are DNA and/or DNA-histone complexes (nucleohistone). Here detailed examinations of the target antigens were carried out by ELISA, and it was revealed that rabbit sera contained three types of antibodies: antibodies reacting equally with both dsDNA and ssDNA; those reacting with ssDNA alone; and those reacting with nucleohistone. Epitopes recognized by the third type consisted of complexes of dsDNA and H2A + H2B or of dsDNA and H2B. All types of antibodies were antigen specific. Since the diversity of ANA among experimental rabbits was large, it was suggested that genetic background is important in the induction of anti-dsDNA antibodies in this system. Moreover, early induction of antibodies to nucleohistone and the rapid disappearance of ANA suggest that B cell proliferation/maturation for continuous production of ANA requires factors other than RV infection. This system may help elucidate the mechanisms of ANA induction and the development of autoimmune diseases.

Animals↗
PubMed1990

Antiserum raised in pigs against canine distemper virus and its utility in diagnostic procedures for morbillivirus infections (canine distemper, phocine distemper, rinderpest).

Antiserum against canine distemper virus (CDV) was raised in pigs by intranasal inoculation with CDV strains CND65 and ROCKBORN. Immunoglobulin fractions were conjugated with horseradish peroxidase. Peroxidase-conjugated anti-CDV immunoglobulin preparations were used for the detection and titration of CDV, seal-derived (phocine) distemper virus (PDV) and rinderpest virus (RPV) in Vero cell cultures. For the detection and titration of corresponding neutralizing antibodies a direct neutralizing peroxidase-linked antibody (NPLA) assay was established. The results were compared with those obtained with the conventional microtitre neutralization test (MNT) based on CPE reading. In addition the sensitivity of an indirect peroxidase-linked antibody (PLA) assay was tested in parallel with that of the NPLA assay using sera obtained from CDV-immunized pigs.

Animals↗
PubMed2004

Characterization of immunodominant linear B-cell epitopes on the carboxy terminus of the rinderpest virus nucleocapsid protein.

The nucleocapsid (N) protein of rinderpest virus (RPV) is one of the most abundant and immunogenic viral proteins expressed during natural or experimental infection. To identify immunogenic epitopes on the N protein, different forms of RPV N protein, including the full-length protein (N(1-525)), an amino-terminal construct (N(1-179)), and a carboxy-terminal construct (N(414-496)), were expressed in Escherichia coli as glutathione S-transferase (GST) fusion proteins. The antigenicity of each recombinant protein was evaluated by Western immunoblotting. All recombinants were recognized by hyperimmune RPV bovine antisera, indicating that immunoreactive epitopes may be present at both ends of the N protein. However, GST-N(414-496) was much more antigenic than GST-N(1-179) when tested with sera from vaccinated cattle, suggesting that an immunodominant or highly immunogenic epitope(s) may be located at the carboxy terminus of the N protein. Epitope mapping with overlapping peptides representing different regions of the carboxy terminus (amino acids 415 to 524) revealed three nonoverlapping antigenic sites in regions containing the residues (440)VPQVRKETRASSR(452) (site 1), (479)PEADTDPL(486) (site 2), and (520)DKDLL(524) (site 3). Among these, antigenic site 2 showed the strongest reactivity with hyperimmune anti-RPV bovine sera in a peptide enzyme-linked immunosorbent assay but did not react with hyperimmune caprine sera raised against peste-des-petits-ruminants virus, which is antigenically closely related to RPV. Identification of an immunodominant linear antigenic site at the carboxy terminus of the N protein may provide an antigen basis for designing diagnostics specific for RPV.

Animals↗
PubMed1976

Autoimmunity induced in rabbits by rinderpest virus.

During rinderpest virus infection in rabbits, 19S cold hemagglutinating antibody against rabbit erythrocytes and 7S anti-nuclear antibody, which reacts with the nuclei and/or the nuclear membranes in immunofluorescent staining, were demonstrated. Virus infection that affected the thymus-dependent immune functions was speculated to act as a trigger for the production of these two autoantibodies.

Animals↗
PubMed2003

Competitive enzyme-linked immunosorbent assay based on monoclonal antibody and recombinant hemagglutinin for serosurveillance of rinderpest virus.

A competitive enzyme-linked immunosorbent assay (C-ELISA) which detects antibodies unique to rinderpest virus (RPV) has been developed. This test can differentiate antibodies against RPV and those against peste des petits ruminants virus. The recombinant RPV hemagglutinin (H)-protein C-ELISA (recH C-ELISA) is based on the ability of a well-characterized monoclonal antibody (MAb) produced with the soluble, secreted form of the H protein (Sec H protein) of RPV made in a baculovirus expression system to compete with the binding of RPV antibodies in the serum of vaccinated or infected, recovered animals to the Sec H protein. The B-cell epitope recognized by the MAb corresponds to amino acids 575 to 583 on the H protein, which is not present on the antigenically closely related peste des petits ruminants virus hemagglutinin-neuraminidase protein. Initially, a positive-negative threshold cutoff value for percent inhibition of 34 was established with 500 known RPV-negative serum samples. The recH C-ELISA was developed with the enzyme immunoassay software of a commercial RPV C-ELISA kit. Comparative analysis of the test results for 700 serum samples obtained with the commercial kit gave a sensitivity of 112.4% and a specificity of 72.4%. Variations in percent inhibition values were observed for the two assay systems. These variations may have been due to the undefined amount of antigen present in the commercial kit as well as the use of a different MAb. The recH C-ELISA detected more positive serum samples compared to the number detected by the commercial kit, with the results confirmed by a virus neutralization test. Thus, recH C-ELISA is a sensitive tool for RPV serosurveillance in disease eradication programs.

Animals↗
PubMed2006

Rinderpest virus blocks type I and type II interferon action: role of structural and nonstructural proteins.

Rinderpest virus (RPV) is a paramyxovirus closely related to the human pathogen Measles virus. It causes severe disease in cattle, buffalo, and some wild animals; although it can infect humans, it does not cause disease. Here, we demonstrate that RPV blocks the action of both type I (alpha) and type II (gamma) interferons (IFNs) by blocking the phosphorylation and nuclear translocation of STAT1 and STAT2 and that this block is not related to species specificity. In addition, both wild-type virulent and vaccine strains of the virus blocked IFN action. Unlike the case with some other paramyxoviruses, neither STAT1 nor STAT2 is degraded upon virus infection. STAT1 is bound by both the viral structural protein P, and thereby recruited to concentrations of viral protein in the cell, and the nonstructural protein V. Although both P and V proteins bind to STAT1 and can block IFN action when expressed in transfected cells, the IFN antagonist activity of the P protein is weaker than that of the V protein. The viral C protein also seems to weakly block IFN-induced activation of STAT1 in transfection experiments. However, studies with knockout viruses showed that the viral V protein appears to be the dominant inhibitor of IFN signaling in the context of virus infection, since prevention of viral V expression restored the IFN sensitivity of infected cells. Although a change in the distribution pattern of STAT2 was observed in virus-infected cells, STAT2 was not bound by any viral protein.

Animals↗
PubMed1996

Relative ability of different bovine leukocyte populations to support active replication of rinderpest virus.

Bovine peripheral blood mononuclear cells (PBMC) were infected with the pathogenic Saudi isolate of rinderpest virus (RPV) in order to identify the cell subpopulation(s) susceptible to active replication of this virus. Flow cytometry analysis, using a monoclonal antibody recognizing the H glycoprotein of RPV, showed that monocytes were the main subpopulation in which the virus replicated, whereas <2% of lymphocytes expressed viral antigen. The activation of PBMC with concanavalin A before infection resulted in an increase in the capacity of lymphocytes to support RPV replication; >90% of CD4+ and CD8+ T lymphocytes expressed viral antigen at 3 days postinfection, although < or = 40% of gamma/delta T cells were productively infected. B-lymphocyte activation with pokeweed mitogen also resulted in increased replication of this virus in these cells, involving up to 40% of B lymphocytes. An enhancement of lymphocyte susceptibility to infection and active replication by RPV was observed upon coculture of RPV-infected PBMC on bovine endothelial cells. Such enhancement was most marked with the B-cell and CD4+ T-cell subpopulations. Contact between lymphocytes and extracellular matrix components did not alter the capacity of RPV to replicate in lymphocytes. This intercellular contact with endothelial cells increased the viability of certain lymphocyte subpopulations, but it alone could not explain the increased sensitivity to RPV. Intercellular signalling, which resulted in interleukin-2 receptor upregulation, probably played a role. In summary, monocytes are the main target for active, productive infection by RPV. Similar replication in lymphocytes depends on their activation state and on contact with accessory cells such as endothelial cells. These characteristics have important implications for virus traffic in vivo and the pathogenesis of this disease.

Animals↗
PubMed2000

Recovery and characterization of a chimeric rinderpest virus with the glycoproteins of peste-des-petits-ruminants virus: homologous F and H proteins are required for virus viability.

Rinderpest (RP) and peste-des-petits-ruminants (PPR) are two important diseases of domestic ruminants. To improve on currently available vaccines against PPR, we have created cDNA copies of the RP virus genome in which either the fusion (F) or hemagglutinin (H) gene, or both, was replaced with the corresponding gene from PPR virus. It was necessary to develop a modified rescue system in which the T7 RNA polymerase was provided by a recombinant fowlpox virus and the entire rescue procedure took place in Vero cells before we could obtain live virus from these chimeric constructs. No virus was recovered when only one of the glycoprotein genes was changed, but a chimeric virus containing both F and H genes from PPR virus was reproducibly rescued from cDNA, indicating that a virus-specific functional interaction takes place between the F and H proteins. The rescued virus expressing the PPR glycoproteins grew more slowly in tissue culture than either parental virus and formed abnormally large syncytia. Goats infected with the chimera showed no adverse reaction, as assessed by clinical signs, temperature, leukocyte count, virus isolation, and serology, and were protected from subsequent challenge with wild-type PPR virus.

Animals↗
PubMed1975

A study of immunoglobulin M antibody to measles, canine distemper, and rinderpest viruses in sera of patients with subacute sclerosing panencephalitis.

Seven boys were studied who had the clinical features of subacute sclerosing panencephalitis (SSPE) and whose brain histology was consistent with SSPE. Measles antigen was detected in the seven brains by the direct fluorescent antibody method. Three out of the seven boys had in their sera measles specific immunoglobulin M (IgM) which was detected by the indirect fluorescent antibody method, and the cell receptors for it were acetone stable. A prozone effect was noted in the sera of two patients. The absorption of one patient's serum with Staphylococcus aureus to reduce the titre of immunoglobulin G (IgG) removed the prozone effect. Two of the boys who had high titres of measles specific IgM also had serum IgM which reacted with canine distemper virus antigen but the titres were eightfold lower. None of the boys had detectable rinderpest specific IgM in their sera.

Adolescent↗
PubMed1994

Rapid differential diagnosis of rinderpest and peste des petits ruminants using an immunocapture ELISA.

An immunocapture ELISA for the diagnosis of rinderpest and peste des petits ruminants is described. Monoclonal antibodies directed against non-overlapping antigenic domains on the nucleocapsid (N) were used to detect the virus N protein in supernatants from infected cells and in field specimens. The assay, which is very sensitive, can be performed in one hour on pre-coated plates. There was no cross reaction between the two viruses in the test and the N protein could be detected in infected cell supernatants kept at ambient temperature for one week. These results show that the ELISA is suitable for routine diagnosis of field samples.

Animals↗