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Melkote S. Shaila - One of the best experts on this subject based on the ideXlab platform.
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Host factor Ebp1 inhibits Rinderpest Virus transcription in vivo
Archives of Virology, 2010Co-Authors: M. Gopinath, S Raju, Ayae Honda, Melkote S. ShailaAbstract:ErbB3 binding protein Ebp1 has been shown to downregulate ErbB3 receptor-mediated signaling to inhibit cell proliferation. Rinderpest Virus belongs to the family Paramyxoviridae and is characterized by the presence of a non-segmented negative-sense RNA genome. In this work, we show that Rinderpest Virus infection of Vero cells leads to the down-regulation of the host factor Ebp1, at both the mRNA and protein levels. Ebp1 protein has been shown to co-localize with viral inclusion bodies in infected cells, and it is packaged into virions, presumably through its interaction with the N protein or the N-RNA itself. Overexpression of Ebp1 inhibits viral transcription and multiplication in infected cells, suggesting that a mutual antagonism operates between host factor Ebp1 and the Virus.
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Characterization of membrane association of Rinderpest Virus matrix protein.
Biochemical and biophysical research communications, 2007Co-Authors: R. Subhashri, Melkote S. ShailaAbstract:ParamyxoVirus matrix protein is believed to play a crucial role in the assembly and maturation of the Virus particle by bringing the major viral components together at the budding site in the host cell. The membrane association capability of many enveloped Virus matrix proteins has been characterized to be their intrinsic property. In this work, we have characterized the membrane association of Rinderpest Virus matrix (M) protein. The M protein of Rinderpest Virus when expressed in the absence of other viral proteins is present both in the cytoplasm and plasma membrane. When expressed as GFP fusion protein, the M protein gets localized into plasma membrane protrusions. High salt and alkaline conditions resulted in partial dissociation of M protein from cell membrane. Thus, M protein behaves like an integral membrane protein although its primary structure suggests it to be a peripheral membrane protein.
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Phosphoprotein P of Rinderpest Virus binds to plus sense leader RNA: regulation by phosphorylation
Virus research, 2004Co-Authors: Tamal Raha, Rajnish Kaushik, Melkote S. ShailaAbstract:The negative sense genome RNA of Rinderpest Virus, a Paramyxoviridae, is encapsidated with the nucleocapsid protein N and serves as a template for the viral RNA dependent RNA polymerase for transcription and replication. The viral RNA polymerase consists of the large protein L and the phosphoprotein P functioning as the P–L complex. We provide in this report, evidences for specific binding of P protein of Rinderpest Virus to the plus sense leader RNA depending on its phosphorylation status. We have also demonstrated that P protein is released from the le RNA:P protein complex upon phosphorylation in vitro. Finally, we have identified that the C-terminal 358–389 amino acid residues of P protein is involved in le RNA binding. The leader RNA binding may signify a hitherto unidentified role for P protein in the viral RNA synthesis. Moreover, our results indicate a possible role for P protein in the transcription-replication switch through leader RNA binding.
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Leader RNA of Rinderpest Virus binds specifically with cellular La protein: a possible role in Virus replication.
Virus research, 2004Co-Authors: Tamal Raha, Renuka Pudi, Saumitra Das, Melkote S. ShailaAbstract:Rinderpest Virus (RPV) is an important member of the MorbilliVirus genus in the family Paramyxoviridae and employs a similar strategy for transcription and replication of its genome as that of other negative sense RNA Viruses. Cellular proteins have earlier been shown to stimulate viral RNA synthesis by isolated nucleocapsids from purified Virus or from Virus-infected cells. In the present work, we show that plus sense leader RNA of RPV, transcribed from 3' end of genomic RNA,specifically interacts with cellular La protein employing gel mobility shift assay as well as UV cross-linking of leader RNA with La protein.The leader RNA synthesized in Virus-infected cells was shown to interact with La protein by immunoprecipitation of leader RNA bound to La protein and detecting the leader RNA in the immunoprecipitate by Northern hybridization with labeled antisense leader RNA. Employing a minireplicon system, we demonstrate that transiently expressed La protein enhances the replication/transcription of the RPV minigenome in cells. Sub-cellular immunolocalization shows that La protein is redistributed from nucleus to the cytoplasm upon infection. Our results strongly suggest that La protein may be involved in regulation of Rinderpest Virus replication.
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Development of a reconstitution system for Rinderpest Virus RNA synthesis in vitro.
Virus research, 2004Co-Authors: Tamal Raha, Anasuya Chattopadhyay, Melkote S. ShailaAbstract:The RNA dependent RNA polymerase of Rinderpest Virus consists of two subunits—the large protein (L) and the phosphoprotein (P), where L is thought to be responsible for the catalytic activities in association with P protein which plays multiple roles in transcription and replication. The nucleocapsid protein (N) is necessary for encapsidation of genomic RNA, which is required as N–P complex. To understand the different steps of transcription and replication as well as the roles played by the three proteins, an in vitro reconstitution system for RNA synthesis is necessary which is not available for any morbilliVirus. We describe here, an in vitro reconstitution system for transcription and replication of Rinderpest Virus utilizing a synthetic, positive sense N-RNA minigenome template, free of endogenous viral polymerase proteins and recombinant viral proteins (P + L and P + N) expressed in insect cells by recombinant baculoViruses. We show that although L–P complex is sufficient to synthesize negative sense minigenome RNA, soluble N protein is necessary for encapsidation of RNA as well as synthesis of (+) sense leader RNA and (+) sense minigenome RNA.
Thomas Barrett - One of the best experts on this subject based on the ideXlab platform.
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Rinderpest Virus lineage differentiation using rt pcr and snap elisa
Journal of Virological Methods, 2003Co-Authors: Morag A Forsyth, Satya Parida, Graham J Belsham, Soren Alexandersen, Thomas BarrettAbstract:An RT-PCR/ELISA system has been developed that detects and differentiates Rinderpest Virus (RPV) from the other closely related morbilliVirus of ruminants, Peste des petits Ruminants Virus (PPRV). In addition, using lineage specific probes, it is possible to determine whether the Virus sample is wild-type or vaccine, and the likely origin of the outbreak if it is wild-type. It involves carrying out a RT-PCR with one digoxygenin (Dig)-labelled primer followed by a hybridisation step with a Virus-specific, biotin-labelled, probe. The hybridisation step is carried out in an ELISA format on a streptavidin-coated plate. The DIG-labelled products are detected using a specific anti-DIG monoclonal antibody and an anti-mouse horseradish peroxidase conjugate. The hybridisation step replaces nucleotide sequencing or nested PCR for confirmation of the identity of DNA product. The assay is fast and easy to carry out and can give semi-quantitative estimates of the Virus content of samples.
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Rinderpest Virus rpv iscom vaccine induces protection in cattle against virulent rpv challenge
Vaccine, 2001Co-Authors: Hiroshi Kamata, Kazuya Yamanouchi, M S Shaila, Kazue Ohishi, Ellena Hulskotte, Albert D M E Osterhaus, Kenjiro Inui, Thomas BarrettAbstract:Rinderpest Virus (RPV), a member of genus MorbilliVirus in the family Paramyxoviridae, causes an acute and often fatal disease in cattle and other large ruminants. A subunit Rinderpest vaccine consisting of an immune-stimulating complex (ISCOM) incorporating the RPV haemaggulutinin (H) protein, was examined for its ability to induce protective immunity in cattle, the natural host of RPV. All of four cattle vaccinated with the ISCOM vaccine survived challenge with virulent Virus. Three were solidly protected, showing no clinical signs of infection, while the fourth animal developed only mild and transient symptoms. Virus neutralizing antibodies were produced at a significant level in all vaccinated cattle. These results indicate that this ISCOM vaccine is effective in producing protective immunity in cattle and should be a suitable means of delivering glycoprotein antigens from other morbilliViruses.
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Rinderpest Virus infection in primary bovine skin fibroblasts
Archives of virology, 2000Co-Authors: Brett T. Lund, Thomas BarrettAbstract:Rinderpest Virus (RPV) replicated to a high titre in primary bovine skin fibroblats. The course of infection was similar to that seen in established cell lines. Virulent field Virus grew at a faster rate than the fully attenuated vaccine strain of the Virus. Virus antigen expression, as measured by FACScan analysis, correlated with the time course of infection for the two strains in cell cultures. Wild type Virus, obtained directly from cattle, infected cells at a slower rate than Virus passaged even once in primary bovine skin fibroblasts. This is the first report of a productive infection of primary bovine skin fibroblasts by wild type RPV.
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the genome sequence of the virulent kabete o strain of Rinderpest Virus comparison with the derived vaccine
Journal of General Virology, 1996Co-Authors: Michael D. Baron, Yasue Kamata, Valerie Barras, Lynnette C Goatley, Thomas BarrettAbstract: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.
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pathomorphological and immunohistological findings in cattle experimentally infected with Rinderpest Virus isolates of different pathogenicity
Veterinary Microbiology, 1995Co-Authors: Peter Wohlsein, H. M. Wamwayi, G. Trautwein, B. Liess, J Pohlenz, Thomas BarrettAbstract:Experimental infection of nine cattle with seven Rinderpest Virus strains of different pathogenicity resulted in significant variations of clinical signs, morphological lesions and distribution of viral antigen in tissues. The severity of clinical disease was correlated with the extent of tissue alterations and the amount of immunohistologically detectable viral antigen. Both mild and virulent strains of Rinderpest share essentially the same tissue tropisms in vivo, i.e. epithelio- and lympho-tropism. However, Rinderpest Virus isolates of higher pathogenicity showed a more rapid and wider distribution with more extensive lesions than milder strains, which probably accounts for the higher mortality.
Michael D. Baron - One of the best experts on this subject based on the ideXlab platform.
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the Rinderpest Virus non structural c protein blocks the induction of type 1 interferon
Virology, 2009Co-Authors: Emma L Boxer, Sambit K Nanda, Michael D. BaronAbstract:The innate immune response, in particular the production of type 1 interferons, is an essential part of the mammalian host response to viral infection. We have previously shown that Rinderpest Virus, a morbilliVirus closely related to the human pathogen measles Virus, blocks the actions of type 1 and type 2 interferons. We show here that this Virus can also block the induction of type 1 interferon. The viral non-structural C protein appears to be the active agent, since expressing this protein in cells makes them resistant to activation of the interferon-β promoter while recombinant Virus that does not express the C protein activates this promoter much more than Virus expressing the C protein. In addition, differences in activation of the interferon-β promoter by different strains of Rinderpest Virus are reflected in differing abilities of their respective C proteins to block activation of the promoter by dsRNA. The C protein blocks the activation of this promoter induced by either cytoplasmic dsRNA or by Newcastle disease Virus (NDV) infection, as well as activation induced by overexpression of several elements of the signalling pathway, including mda-5, RIG-I and IRF-3. The RPV C protein also blocks transcription from promoters responsive individually to the three transcription factors that make up the interferon-β promoter enhanceosome, although it does not appear to block the activation of IRF-3.
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wild type Rinderpest Virus uses slam cd150 as its receptor
Journal of General Virology, 2005Co-Authors: Michael D. BaronAbstract: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.
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Rinderpest Virus C and V Proteins Interact with the Major (L) Component of the Viral Polymerase
Virology, 2001Co-Authors: David A. Sweetman, James Miskin, Michael D. BaronAbstract:Rinderpest Virus, like other MorbilliViruses, expresses three proteins from the single P gene. In addition to the P protein, which interacts both with the viral polymerase (L) and the nucleocapsid (N) protein, the Virus expresses a C and a V protein from the same gene. The functions of these two proteins in the viral life cycle are not clear. Although both C and V proteins are dispensable, in that viable Viruses can be made that express neither, each seems to play a role in optimum viral replication. We have used the yeast-two hybrid system, binding to coexpressed fusions of C and V to glutathione-S-transferase, and studies of the native size of these proteins to investigate interactions of the Rinderpest Virus C and V proteins with other Virus-encoded proteins. The V protein was found to interact with both the N and L proteins, while the C protein was found to bind to the L protein, and to self-associate in high-molecular-weight aggregates.
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the genome sequence of the virulent kabete o strain of Rinderpest Virus comparison with the derived vaccine
Journal of General Virology, 1996Co-Authors: Michael D. Baron, Yasue Kamata, Valerie Barras, Lynnette C Goatley, Thomas BarrettAbstract: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.
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cloning and sequence analysis of the matrix m protein gene of Rinderpest Virus and evidence for another bovine morbilliVirus
Virology, 1994Co-Authors: Michael D. Baron, Lynette Goatley, Thomas BarrettAbstract:We have cloned and sequenced the entire M gene of the vaccine strain of Rinderpest Virus and that of the virulent Kabete "O" strain from which it was derived. The sequences of these two genes are essentially identical (99% at the nucleotide level), but were very different from a previously published Kabete O M gene sequence (M. Limo and T. Yilma, 1990, Virology 175, 323-327). Inspection of the nucleotide and deduced amino acid sequences of known morbilliVirus M genes showed that the earlier sequence was clearly from a morbilliVirus, but neither from Rinderpest Virus nor from peste des petits ruminants Virus.
M S Shaila - One of the best experts on this subject based on the ideXlab platform.
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expression of hemagglutinin protein of Rinderpest Virus in transgenic tobacco and immunogenicity of plant derived protein in a mouse model
Virology, 2003Co-Authors: Abha Khandelwal, Lakshmi Sita G, M S ShailaAbstract:The use of transgenic plants as a production system for recombinant subunit vaccines has been considered safe and economical compared to cell culture methods. We have exploited this approach to produce Rinderpest Virus hemagglutinin (H) protein in transgenic tobacco as a model plant for testing the immunogenicity of plant-derived hemagglutinin protein. The transgenic nature of the plants was confirmed by molecular analysis such as gene specific PCR and Southern hybridization using full-length H gene as a probe. The Mendelian pattern of inheritance of the transgene has been demonstrated in $T_1$ generation. The transgenic plants express the H protein of molecular weight 72 kDa. The plant derived H protein is antigenically authentic as revealed by reactivity with H-specific antibodies as well as convalescent sera. The induction of immune response was tested in mice after intraperitoneal immunization with plant-derived H. High titers of antibodies were induced which were H-specific and they neutralized the infectivity of Rinderpest Virus.
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expression of hemagglutinin protein of Rinderpest Virus in transgenic pigeon pea cajanus cajan l millsp plants
Plant Cell Reports, 2003Co-Authors: V V Satyavathi, M S Shaila, Abha Khandelwal, V Prasad, Lakshmi G SitaAbstract:Rinderpest Virus is the causative agent of a devastating, often fatal disease in wild and domestic bovids that is endemic in Africa, the Middle East and South Asia. The existing live attenuated vaccine is heat-labile, and thus there is a need for the development of new strategies for vaccination. This paper reports the development of transgenic pigeon pea [Cajanus cajun (L.) Millsp.] expressing one of the protective antigens, the hemagglutinin (H) protein of Rinderpest Virus. A 2-kb fragment containing the coding region of the H protein was cloned into pBI121 and mobilized into Agrobacterium tumefaciens strain EHA105. Embryonic axes and cotyledonary nodes from germinated seeds of pigeon pea were used for transformation. The presence of the transgene in transgenic plants was confirmed by Southern blots, and the specific transcription of the marker gene in the plants was demonstrated by reverse transcription-polymerase chain reaction. Integration of the H gene into the pigeon pea genome was confirmed by Southern hybridization. The expression of the H protein in the transgenic lines was confirmed by Western blot analysis using a polyclonal monospecific antibody to the H protein. The highest level of expression of the hemagglutinin protein in leaves of pigeon pea was 0.49% of the total soluble protein. The transgenic plants were fertile and the transgene expressed in the progeny.
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Rinderpest Virus rpv iscom vaccine induces protection in cattle against virulent rpv challenge
Vaccine, 2001Co-Authors: Hiroshi Kamata, Kazuya Yamanouchi, M S Shaila, Kazue Ohishi, Ellena Hulskotte, Albert D M E Osterhaus, Kenjiro Inui, Thomas BarrettAbstract:Rinderpest Virus (RPV), a member of genus MorbilliVirus in the family Paramyxoviridae, causes an acute and often fatal disease in cattle and other large ruminants. A subunit Rinderpest vaccine consisting of an immune-stimulating complex (ISCOM) incorporating the RPV haemaggulutinin (H) protein, was examined for its ability to induce protective immunity in cattle, the natural host of RPV. All of four cattle vaccinated with the ISCOM vaccine survived challenge with virulent Virus. Three were solidly protected, showing no clinical signs of infection, while the fourth animal developed only mild and transient symptoms. Virus neutralizing antibodies were produced at a significant level in all vaccinated cattle. These results indicate that this ISCOM vaccine is effective in producing protective immunity in cattle and should be a suitable means of delivering glycoprotein antigens from other morbilliViruses.
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mapping of t helper epitopes of Rinderpest Virus hemagglutinin protein
Viral Immunology, 2001Co-Authors: G Sinnathamby, R. Nayak, M S ShailaAbstract:Rinderpest Virus (RPV) is a highly contagious and often fatal disease of domestic and wild ruminants, caused by Rinderpest Virus of the genus MorbilliVirus under the family Paramyxoviridae. Hemagglutinin (H) and fusion (F) proteins of this enveloped Virus confer protective immunity against experimental challenge with virulent Rinderpest Virus. We have earlier demonstrated that immunization with a single dose of recombinant extracellular baculoVirus expressing H protein elicits H-specific humoral and lymphoproliferative responses in cattle. The lymphoproliferative responses are predominantly BoLA class II restricted. In this work, we have analyzed lymphoproliferative responses of peripheral lymphocytes from immunized cattle to truncated H protein fragments expressed in E. coli for locating domains harboring T epitopes. One region (aa 113-182) recognized by immune $T_h$ cells is conserved in the H protein of measles Virus, which was earlier shown to contain a dominant $T_h$ epitope in mouse. Synthetic peptides within this region of measles Virus H protein were used to identify a $T_h$ epitope conserved in the H protein of RPV Virus (aa 123-137) in cattle. A second $T_h$ epitope located at the C-terminus of RPV-H was mapped to the region corresponding to aa 512-609 using truncated protein fragments expressed in E. coli. The C-terminal epitope (aa 575-583) was mapped using synthetic peptides corresponding to measles Virus H as well as RPV-H protein.
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evidence for different lineages of Rinderpest Virus reflecting their geographic isolation
Journal of General Virology, 1993Co-Authors: R. W. Chamberlain, H. M. Wamwayi, M S Shaila, E Hockley, L Goatley, N J Knowles, Thomas BarrettAbstract:Sequence analysis of part of the fusion protein gene from recent isolates of Rinderpest Virus revealed that distinct lineages of the Virus exist which reflect the geographical location of their isolation in Africa and Asia. Current strains circulating in Kenya and Sudan were most similar, both in terms of nucleotide sequence and pathogenic nature, to Viruses isolated in Egypt and in Nigeria in 1983/1984 and they were quite distinct from an East African isolate (RBT-1) from the 1960s. Two older isolates of the Virus, the Japanese avianized/lapinized vaccine strain dating from the 1930s and the Old Kabete strain dating from 1911, each differed considerably from the other Viruses. The sequence data were derived from the region where the precursor protein is cleaved to yield the biologically active F1/F2 heterodimer; all strains analysed had a highly basic connecting peptide which is required for efficient cleavage by endogenous host cell proteases. No correlation was found between amino acid changes at this site and the Rinderpest Virus pathogenicity unlike the association reported for Newcastle disease Virus.
Chieko Kai - One of the best experts on this subject based on the ideXlab platform.
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comparative and mutational analyses of promoter regions of Rinderpest Virus
Virology, 2010Co-Authors: Chieko Imai, Kentaro Fujita, Fusako Shimizu, Akihiro Sugai, Misako Yoneda, Chieko KaiAbstract:Comparative and mutational analysis of promoter regions of Rinderpest Virus was conducted. Minigenomic RNAs harboring the genomic and antigenomic promoter of the lapinized virulent strain (Lv) or an attenuated vaccine strain (RBOK) were constructed, and the expression of the reporter gene was examined. The activities of the antigenomic promoters of these strains were similar, whereas the activity of the genomic promoter (GP) of the RBOK strain was significantly higher than that of the Lv strain, regardless of cell type and the source of the N, P and L proteins. Increased replication (and/or encapsidation) activities were observed in the minigenomes that contained RBOK GP. Mutational analysis revealed that the nucleotides specific to the RBOK strain are responsible for the strong GP activity of the strain. It was also demonstrated that other virulent strains of RPV (Kabete O, Saudi/81 and Kuwait 82/1) have weaker GPs than that of the RBOK strain.
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Molecular properties of the matrixprotein(M) gene of the lapinized Rinderpest Virus.
The Journal of veterinary medical science, 2001Co-Authors: Motohiro Shiotani, Ryuichi Miura, Kentaro Fujita, Chiaki Wakasa, Masashi Uema, Chieko KaiAbstract:The nucleotide sequence of the matrixprotein (M) gene of the lapinized Rinderpest Virus (RPV-L) was determined. The full-length cDNA of the RPV-L M gene is composed of 1460 base pairs and is supposed to contain an open reading frame of 1005 nucleotides encoding on M protein of 335 amino acids. The homology of the predicted amino acid among congeneric morbilliViruses such as RPV Kabete `O' strain (wild strain of RPV), RPV RBOK strain (vaccine strain of RPV for cattle), measles Virus (MV), and canine distemper Virus (CDV), is approximately 94%, 93%, 87% and 77%, respectively. In the present study, all coding regions of the RPV-L strain have been determined.
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Immunizing effect of vaccinia Virus expressing the nucleoprotein of Rinderpest Virus on systemic Rinderpest Virus infection in rabbits.
Comparative immunology microbiology and infectious diseases, 1998Co-Authors: Kazuya Nakamura, Kazuya Yamanouchi, Hiroshi Kamata, Kazue Ohishi, Shigetoshi Ohkubo, Kosaku Fujiwara, Chieko KaiAbstract:A recombinant vaccinia Virus (RVV) expressing the nucleoprotein (NP) of Rinderpest Virus (RPV) was examined in rabbits for the involvement of the NP protein in protection from the RPV infection. Despite their production of anti-NP antibody, the RVV-immunized rabbits succumbed to the RPV challenge, although there was a slight delay in the onset of disease after the low-dose challenge. On the other hand, the animals immunized with RVV expressing the hemagglutinin (H) protein of the RPV were completely protected. These results indicate that the NP protein might be not so effective as the H protein for the protection against viremic and systemic infection with RPV.
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Construction of Recombinant Vaccinia Virus Expressing Rinderpest Virus Nucleocapsid Protein and Its Immunogenicity in Mice
The Journal of veterinary medical science, 1998Co-Authors: Kazue Ohishi, Kazuya Yamanouchi, Hiroshi Kamata, Shigetoshi Ohkubo, Chieko KaiAbstract:Recombinant vaccinia Virus (rVV) was constructed by inserting Rinderpest Virus (RPV) nucleocapsid (N) protein gene. The rVV expressed RPV-N protein in the rVV-infected cells. The rVV was shown to produce RPV-N-specific antibody in mice.
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Immunohistochemical studies of lymphoid tissues of rabbits infected with Rinderpest Virus.
Journal of comparative pathology, 1995Co-Authors: Masatsugu Okita, Kazuya Yamanouchi, Takeshi Mori, Yeon-sil Shin, Masayuki Miyasaka, Takeshi Mikami, Chieko KaiAbstract:Summary The pathogenesis of infection with the L-strain of Rinderpest Virus (RPV) in rabbits was investigated. Of several lymphoid tissues examined, those associated with the gut showed the most marked Virus growth. The Virus titres were maximal 4 days after inoculation but had declined at day 6. The distribution of viral antigen was examined immunohistochemically with the recently established anti-rabbit CD5 monoclonal antibody (MoAb), which is a pan-T-cell marker, and the anti-RPV-nucleoprotein MoAb. The Virus antigen was localized in the CD5+ area at the initial stage of infection but spread to all areas of the lymphoid tissues at the later stages. By flow cytometric analysis with both rabbit CD5 and CD4 MoAbs, a decrease of the CD4+ and CD5+ subpopulations was observed in the spleen and mesenteric lymph nodes.
