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PubMed1995

Sequencing and analysis of the nucleocapsid (N) and polymerase (L) genes and the terminal extragenic domains of the vaccine strain of rinderpest virus.

The nucleocapsid (N) and polymerase (L) genes of the vaccine strain of rinderpest, and the 5' and 3' terminal domains of the genome have been sequenced. Together with previously published data, this completes the sequence of the entire genome of rinderpest virus. The viral genome is 15,881 bases in length, similar to that of measles virus and slightly longer than that of canine distemper virus. The L gene is identical in length to that of measles virus, encoding a 2183 amino acid protein with a calculated M(r) of 248,100. The L protein sequence of morbilliviruses is highly conserved, more than 75% of residues being identical or conserved in all three sequences currently available. The N protein was, as for the other sequenced genes where comparison is possible, essentially identical to that of the virulent parent. In addition, we have determined the terminal sequences of two virulent strains of rinderpest and compared the sequences of virulent and non-virulent strains.

Amino Acid Sequence↗
PubMed1999

Cell-mediated immune responses in cattle vaccinated with a vaccinia virus recombinant expressing the nucleocapsid protein of rinderpest virus.

Rinderpest virus (RPV) is a member of the genus Morbillivirus in the family Paramyxoviridae which causes an acute and often fatal disease in large ruminants. To examine the immune response to the virus nucleocapsid (N) protein, a recombinant vaccinia virus expressing RPV nucleocapsid protein (rVV-RPV-N) was used to vaccinate cattle. The recombinant vaccine induced low levels of non-neutralizing anti-N antibodies. RPV-specific cell-mediated immunity induced by the recombinant was assessed by measuring both the lymphocyte proliferation and cytotoxic T-lymphocyte responses. The protective immune response was examined by challenging the vaccinated cattle with either a highly virulent (Saudi 1/81) or a mild (Kenya/eland/96) strain of the virus. The vaccinated cattle were not protected against challenge with the virulent RPV strain, except they showed a slight delay in the onset of disease when compared with the unvaccinated controls. In cattle challenged with the mild strain, apart from a transient fever, no clinical signs of rinderpest infection were seen in the vaccinated cattle. One out of two control cattle showed a similar response but the other died from classic rinderpest disease. Virus-neutralizing antibodies were induced more quickly following challenge with the mild strain in vaccinated cattle compared to the control animals. These data suggested that the cell-mediated immunity induced by rVV-RPV-N could stimulate the rapid production of neutralizing antibodies following RPV challenge but this response was not sufficient to protect against challenge with a virulent strain of the virus. Protection was seen in one of three animals challenged with a mild strain of the virus; however, a greater number of animals would need to be tested to estimate the significance of the protection afforded by the N protein.

Animals↗
PubMed1988

Protection of cattle against rinderpest with vaccinia virus recombinants expressing the HA or F gene.

Rinderpest is a highly contagious ruminant viral disease manifested by a rapid course and greater than 90% mortality. Infectious vaccinia virus recombinants were constructed that express either the hemagglutinin or the fusion gene of rinderpest virus. All cattle vaccinated with either recombinant or with the combined recombinants produced neutralizing antibodies against rinderpest virus and were protected against the disease when challenged with more than 1000 times the lethal dose of the virus.

Animals↗
PubMed1997

Rescue of rinderpest virus from cloned cDNA.

Rinderpest virus is a morbillivirus and is the causative agent of a widespread and important disease of cattle. The viral genome is a single strand of RNA in the negative sense. We have constructed plasmids containing cDNA copies of the 5' and 3' termini of the virus separated by a reporter gene and have shown that antigenome-sense RNA transcripts of these model genomes can be replicated, transcribed, and packaged by helper virus, both rinderpest virus and the related measles virus. Further, these genome analogs can be replicated and transcribed by viral proteins expressed from cDNA clones by using a recombinant vaccinia virus expressing T7 RNA polymerase (MVA-T7). Using this latter system, we have rescued live rinderpest virus from a full-length cDNA copy of the genome of the RBOK vaccine strain. The recombinant virus appears to grow in tissue culture identically to the original virus.

Animals↗
PubMed2000

Rinderpest viruses lacking the C and V proteins show specific defects in growth and transcription of viral RNAs.

Rinderpest virus is a morbillivirus and the causative agent of an important disease of cattle and wild bovids. The P genes of all morbilliviruses give rise to two proteins in addition to the P protein itself: use of an alternate start translation site, in a second open reading frame, gives rise to the C protein, while cotranscriptional insertion of an extra base gives rise to the V protein, a fusion of the amino-terminal half of P to a short, highly conserved, cysteine-rich zinc binding domain. Little is known about the function of either of these two proteins in the rinderpest virus life cycle. We have constructed recombinant rinderpest viruses in which the expression of these proteins has been suppressed, individually and together, and studied the replication of these viruses in tissue culture. We show that the absence of the V protein has little effect on the replication rate of the virus but does lead to an increase in synthesis of genome and antigenome RNAs and a change in cytopathic effect to a more syncytium-forming phenotype. Virus that does not express the C protein, on the other hand, is clearly defective in growth in all cell lines tested, and this defect appears to be related to a decreased transcription of mRNA from viral genes. The phenotypes of both individual mutant virus types are both expressed in the double mutant expressing neither V nor C.

Animals↗
PubMed1995

[Evaluation of vaccinal protection against rinderpest in Cameroon. II. The North province].

Cameroon joined the sero-survey component of the PARC (Pan African Rinderpest Campaign) program in 1989. During the 1992 Campaign, a detailed sampling frame, adapted to the breeding conditions of the North Province was drawn up according to PARC recommendations. The four administrative divisions of the province were covered by sampling cattle in 14 sites chosen by randomisation. Eight thousand six hundred and eighty sera samples from 217 cattle herds were tested using FAO/IAEA rinderpest competitive ELISA technique. The results indicated an overall prevalence of rinderpest virus antibodies (RPVA) of 66%. This is below the target objective. The differences of prevalence between age groups and breeding systems (sedentary of transhumant) are statistically significant. The same results have been reported in the Adamaoua Province (62% in 1991 campaign). These results do not reflect the situation in all the country. It is suggested to hold general meeting between different livestock managers from the provinces with high cattle populations to adopt commun vaccination measures with the target objective of increasing the level of immunity.

Animals↗
PubMed1998

Recommended standards for epidemiological surveillance systems for rinderpest. Office International des Epizooties.

A process involving time-bound steps used to verify the transition from the status of freedom from rinderpest to that of freedom from infection with the rinderpest virus is described. The procedure, informally but widely known as the 'OIE Pathway' (OIE: Office International des Epizooties), originated with the report of the 1989 Expert Consultation on Rinderpest Surveillance Systems. The OIE Foot and Mouth Disease and Other Epizootics Commission, with the assistance of experts on the disease, proposed a revision of the recommended standards in the reference document presented at the 66th General Session of the OIE (66 SG/12/CS3 B, Appendix III). During that General Session, the standards were amended and adopted by the OIE International Committee (Resolution No. IX dated 28 May 1998).

Animals↗
PubMed2001

Identification of a cytotoxic T-cell epitope on the recombinant nucleocapsid proteins of Rinderpest and Peste des petits ruminants viruses presented as assembled nucleocapsids.

The nucleocapsid protein (N) of morbilliviruses is not only a major structural protein but also the most abundant protein made in infected cells. We overexpressed the N proteins of Rinderpest virus and Peste des petits ruminants virus in E. coli, which assemble into nucleocapsids in the absence of viral RNA that resemble nucleocapsids made in the virus-infected cells. Employing these assembled structures resembling subviral particles, we studied the induction of both the antibody response and the cytotoxic T-lymphocyte (CTL) response in a murine model (BALB/c). A single dose of the purified recombinant nucleocapsids of both viruses in the absence of an adjuvant induces a strong CTL response. The CTLs generated are antigen specific and cross-reactive with respect to each virus and, furthermore, this CTL response is MHC class I restricted. Based on the prediction for H-2(d)-restricted T-cell motifs we tested the lysis of transfected P815 (H-2(d)) cells expressing a nine amino acid potential CTL epitope, by splenic T cells in vitro restimulated with bacterially expressed RPV or PPRV N proteins. We extended our study to the bovine system both to analyze the immunogenicity of these recombinant proteins in the natural hosts and to show that PBMC from cattle vaccinated with Rinderpest vaccine proliferate in vitro, in response to restimulation with soluble nucleocapsid proteins. Furthermore, the murine CTL epitope functions in the bovine system as a cytotoxic T-cell epitope. 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.

Amino Acid Motifs↗
PubMed1989

Development of heat-stable recombinant rinderpest vaccine.

Recombinant vaccinia virus (RVV) containing the full-length cDNA of rinderpest virus (RV)-haemagglutinin (H) gene was constructed. The H gene was inserted into the attenuated vaccine strain of vaccinia virus (VV), Le 16 m0, with two different promoters, namely cowpox virus A-type inclusion body (ATI) promoter or VV 7.5 kilodalton (P7.5) promoter. These RVVs produced the same sized fully glycosylated RV-H protein in RK 13 cells as that of the authentic RV-H. Their heat stability in the lyophylized state was similar to that of the parental VV. All rabbits immunized with these RVVs produced virus neutralizing (VN) antibody to RV as well as anti RV-H antibody. Four weeks after immunization, these animals were challenged with RV intravenously. None of the RVV-immunized rabbits developed any clinical signs of RV infection except one which was immunized with RVV containing the ATI promoter and developed low VN titer. These results indicate the possibility of developing a heat-stable recombinant vaccine for the eradication of rinderpest in tropical countries without cold storage systems.

Animals↗
PubMed1991

Immunological and virological characterization of improved construction of recombinant vaccinia virus expressing rinderpest virus hemagglutinin.

We constructed a recombinant vaccinia virus (RVV) expressing rinderpest virus (RPV) hemagglutinin (H) by modifying the promoter region of the original RVV. The promotor region was modified at three points, i.e., an outframe ATG was eliminated, the sequence between the promoter and initiation codon was shortened and the base sequence just upstream of the initiation codon was changed. As compared with the original RVV, the modified RVV was found to produce a remarkably large amount of H protein in infected rabbit kidney cells cultured in vitro and to induce high titers of anti-RPV-H antibodies in rabbits. The median protective doses in rabbits of the modified and of the original RVVs were 10(2) pfu and 10(3.5) pfu, respectively, indicating that the modified RVV was at least 10-times more effective in protection than the original. The neurovirulence of the modified RVV and the parental LC16mO strain was roughly at the same level, and was much lower than that of WR strain. The modified RVV was as heat-stable as the original one. These results indicate that the modified RVV could be a candidate rinderpest vaccine for further examinations including cattle.

Animals↗
PubMed1984

The shedding of a virulent Kabete O strain of rinderpest virus by cattle.

A Muguga substrain of the virulent Kabete O strain of rinderpest virus was demonstrated in the ocular, nasal, oral and rectal swabs collected from infected cattle. Ocular shedding was detected at the onset of viraemia and before the onset of clinical signs whilst virus shedding in nasal, oral and rectal discharges appeared at the same time as lesions. It is suggested that virus isolation from ocular and nasal swabs should be considered in the diagnosis of rinderpest in addition to the other methods currently employed, as virus was isolated from swabs collected from dead animals.

Animals↗
PubMed1989

An epidemiological model of rinderpest. I. Description of the model.

The development of an epidemiological model of rinderpest in cattle and wildlife populations is described. The model uses a state-transition structure, incorporating a stochastic element through the use of Monte-Carlo methods modified to allow large populations to be simulated. The potential applications include the estimation of "safe" host population immunity rates and the design of cost-effective rinderpest vaccination programmes.

Animals↗
PubMed1986

Single radial hemolysis test for the detection of rinderpest antibody.

The single radial hemolysis [SRH] test was employed for detection of rinderpest antibodies in post-vaccinated serum samples as also in serum samples from animals recovered from rinderpest infection. The results were compared with counterimmunoelectrophoresis [CIE] and serum neutralisation [SN] tests. The CIE test was found to be more sensitive than SRH but because of ease and simplicity SRH can also be used for monitoring antibody development after vaccination.

Animals↗
PubMed1986

Simple and rapid dot-enzyme immunoassay for visual detection of rinderpest antibodies in bovine and caprine sera.

A modified solid phase enzyme immunoassay (EIA) is described for visual detection of anti-rinderpest virus (RPV) antibodies in cattle and goat sera. Dots of RPV antigens were adsorbed to nitrocellulose (NC) paper (hence Dot-EIA) and the adsorptive reactive sites were blocked with skim milk powder. After immersion in bovine or caprine test serum bound antibodies were reacted with a peroxidase-conjugated anti-bovine or anti-caprine IgG (H & L), respectively. Positive reactions were easily visualized as red-brown dots after enzyme degradation of a substrate containing hydrogen peroxide and amino-ethylcarbazole (AEC). The Dot-EIA was comparable to the serum neutralisation (SN) test in its ability to detect antibody in bovine sera seven or ten days after experimental infection (DPI) with live attenuated Kabete "O" (RBOK) strain of RPV (grown in Vero cells) by a combination of subcutaneous (s/c), intravenous (i/v) or intranasal (i/n) routes. Early (seven DPI) RPV antibodies were detected in a serum sample from one goat experimentally infected with RPV by combined s/c-i/v routes but not in another goat only infected intranasally. The specificity of the Dot-EIA was equal to that of the SN test, as serum samples, collected from these experimental animals and those inoculated with non infected Vero cell culture fluid, with SN titres of 0.3 or lower were all negative by Dot-EIA. The Dot-EIA may have potential application as a rapid, simple and economical field test in diagnosis of rinderpest, vaccination surveillance and other seroepidemiological studies.

Animals↗
PubMed1986

Development and stability of rinderpest virus antigens in cattle tears and lymph nodes.

Diffusible rinderpest virus antigens were demonstrated in increasing quantities in ocular and lymph node biopsies from rinderpest-infected cattle using agar gel immunodiffusion (AGID) and counterimmunoelectrophoresis (CIEP) tests. Positive samples were detected from the second day of pyrexia to two days after death. The antigens in ocular secretions and lymph nodes were thermolabile being destroyed within five minutes at 56 degrees C and within two weeks at 4 degrees C.

Animals↗
PubMed1993

Single capripoxvirus recombinant vaccine for the protection of cattle against rinderpest and lumpy skin disease.

A recombinant capripoxvirus has been constructed containing a full-length cDNA of the fusion protein gene of rinderpest virus. The gene was inserted in the thymidine kinase gene of the capripox genome under the control of the vaccinia virus major late promoter p11 together with the Escherichia coli gpt gene in the opposite orientation under the control of the vaccinia early/late promoter p7.5. A vaccine prepared from this recombinant virus protected cattle against clinical rinderpest after a lethal challenge with a virulent virus isolate. In addition, the vaccine protected the cattle against lumpy skin disease.

Animals↗
PubMed1993

Antibody levels determined by an appropriate technology (HI) in local cattle following anti-rinderpest campaign in Nigeria.

The levels of antibodies against rinderpest measured by the haemagglutination inhibition (HI) test were titrated in 640 randomly collected sera. Out of 640 samples, 586 (91%) exhibited high titres of > 4 while 54 (9%) had low titres of < or = 4. Of the 400 samples collected in Zaria, 354 (88.5%) had high titres while 46 (11.5%) had low titres. In Funtua, 140 samples were collected with 132 (94.3%) recording high titres while 8 (5.7%) had low titres. All samples (100) collected from Shika had high titres (100%). Statistical evaluation with analysis of variance and Tukey's HSD tests showed no significant difference at the alpha = 0.05 level of significance between mean antibody titres in the areas under investigation; this showed the vaccines used during the anti-rinderpest campaign to be of good immunogenic quality.

Animals↗