Immune response and protection of cattle and pigs generated by a vaccinia virus recombinant expressing the F protein of rinderpest virus

Belsham, Graham J.; Anderson, E. C.; Murray, P.K.; Anderson, Joseph R.; Barrett, Tom

doi:10.1136/vr.124.25.655

Cited by 36 publications

(17 citation statements)

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“…Protection against rinderpest using recombinant vaccinia viruses expressing the H or F gene of RPV has been described recently Barrett et al, 1989;Belsham et al, 1989;Tsukiyama et al, 1989). However, detailed antigenic and functional analyses of these proteins have not been reported, with the exception of a few preliminary studies (Bhavani et al, 1989;Sugiyama et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

Antigenic and Functional Characterization Of Rinderpest Virus Envelope Proteins Using Monoclonal Antibodies

Sugiyama

Minamoto

Kinjo

et al. 1991

Journal of General Virology

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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 morbiUiviruses. The anti-H and anti-F MAbs defined seven and three distinct antigenic sites, respectively. The MAbs to six sites on H were able to neutralize the infectivity of RPV. The addition of guinea-pig complement or anti-mouse immunoglobulin increased the virus-neutralizing antibody titre of most of the anti-H MAbs, including those lacking neutralizing activity. One of the antigenic sites on H was conserved among morbilliviruses and the MAbs to this site had haemagglutination inhibition activity against measles virus (MV). The remaining sites were specific for RPV and varied antigenically between strains of RPV. The anti-F MAbs lacked neutralizing activity, but two of the five MAbs did show activity in the presence of complement or anti-mouse immunoglobulin. On the whole, the antigenic sites on F were conserved in some strains of MV, but not in canine distemper virus. All of the sites on the surface proteins were sensitive to SDS and, although those on F were not affected by 2-mercaptoethanol, five of the seven sites on H were destroyed by it. These results suggest that the epitopes on the envelope proteins are conformation-dependent.

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Section: Introductionmentioning

confidence: 99%

Antigenic and Functional Characterization Of Rinderpest Virus Envelope Proteins Using Monoclonal Antibodies

Sugiyama

Minamoto

Kinjo

et al. 1991

Journal of General Virology

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“…Morbilliviruses have six structural proteins, namely the attachment or haemagglutinin protein (H), the fusion protein (F), the matrix protein (M), the phosphoprotein (P), the polymerase protein (L) and the nucleocapsid protein (N). Recombinant poxviruses expressing either the RPV H or F protein have been shown to protect cattle from challenge with a lethal dose of virulent RPV, indicating the importance of the virus surface glycoproteins in generating a protective immune response (Belsham et al, 1989 ;Yamanouchi et al, 1993 ;Yilma et al, 1988). In some cases, cattle with very low neutralizing antibody titres following vaccination, or even some which were without detectable neutralizing antibody, were shown to be protected against the challenge.…”

Section: Introductionmentioning

confidence: 99%

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

Ohishi

Inui

Yamanouchi

et al. 1999

Journal of General Virology

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Rinderpest virus (RPV) is a member of the genus Morbillivirus in the familyParamyxoviridae 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 nonneutralizing 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.

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“…The nucleocapsid is in turn surrounded by a lipid envelope which contains two glycoproteins, F (fusion) and H (attachment). It is known that these glycoproteins are the major protective immunogens and are responsible for inducing neutralizing antibodies (6,22,49,50). The high degree of sequence conservation between the F proteins of different morbilliviruses (9,30) probably accounts for the extensive cross-protection observed between different viruses of this genus, enabling, for example, the RPV vaccine to be used to vaccinate against PPRV.…”

mentioning

confidence: 99%

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

Das

Baron

Barrett

2000

J Virol

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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.

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Immune response and protection of cattle and pigs generated by a vaccinia virus recombinant expressing the F protein of rinderpest virus

Cited by 36 publications

References 0 publications

Antigenic and Functional Characterization Of Rinderpest Virus Envelope Proteins Using Monoclonal Antibodies

Antigenic and Functional Characterization Of Rinderpest Virus Envelope Proteins Using Monoclonal Antibodies

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

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

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