Preparation and characterization of monoclonal antibodies to nucleocapsid protein N and H glycoprotein of rinderpest virus

Bhavani, K.; Karande, Anjali A.; Shaila, M.S.

doi:10.1016/0168-1702(89)90091-9

Cited by 14 publications

(5 citation statements)

References 22 publications

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“…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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“…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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“…Three weeks after the second booster, mice were further boosted with 100 g of purified Sec H intraperitonealy. Four days later, one of the immunized animal was sacrificed to make a spleen cell suspension which was fused with Sp2/0 myeloma cells by standard PEG-mediated fusion as described by Bhavani et al (1989).…”

Section: Generation Of Rpv-h Hybridoma Clonesmentioning

confidence: 99%

“…We and others (Bhavani et al, 1989;Sugiyama et al, 1989;Anderson and McKay, 1994) have earlier reported the production and characterization of a panel of mAbs to H protein. However, the linear and/or conformational epitopes for these mAbs were not mapped on the protein, which could provide an insight into the antigenic structure of the protein.…”

Section: Introductionmentioning

confidence: 99%

Mapping of B-Cell Epitopes of Hemagglutinin Protein of Rinderpest Virus

et al. 2002

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Monoclonal antibodies (mAbs) against secreted hemagglutinin (H) protein of rinderpest virus (RPV) expressed by a recombinant baculovirus were generated to characterize the antigenic sites on H protein and regions of functional significance. Three of the mAbs displayed hemagglutination inhibition activity and these mAbs were unable to neutralize virus infectivity. Western immunoblot analysis of overlapping deletion mutants indicated that three mAbs recognize antigenic regions at the extreme carboxy terminus (between amino acids 569 and 609) and the fourth mAb between amino acids 512 and 568. Using synthetic peptides, aa 569-577 and 575-583 were identified as the epitopes for E2G4 and D2F4, respectively. The epitopic domains of A12A9 and E2B6 mAbs were mapped to regions encompassing aa 527-554 and 588-609. Two epitopes spanning the extreme carboxy terminal region of aa 573 to 587 and 588 to 609 were shown to be immunodominant employing a competitive ELISA with polyclonal sera form vaccinated cattle. The D2F4 mAb which recognizes a unique epitope on RPV-H is not present on the closely related peste des petits ruminant virus HN protein and this mAb could serve as a tool in the seromonitoring program after rinderpest vaccination.

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“…Ils ont été appliqués de façon systématique à l'analyse des différences antigéniques existant au sein des morbillivirus. Des batteries d'AcM ont permis d'étudier chaque membre du genre Morbillivirus : CDV (30), MV (6,29,36,38,44), RPV (5,24,26,27,41,42) et PPRV (35). Une variation antigénique plus importante que celle observée précédemment avec les anticorps polyclonaux a pu être décelée.…”

Section: S Introductionunclassified

Caractérisation d'anticorps monoclonaux dirigés contre les virus de la peste bovine et de la peste des petits ruminants : identification d'épitopes conservés ou de spécificité stricte sur la nucléoprotéine

Libeau

Saliki²,

Diallo³

1997

Rev. Elev. Med. Vet. Pays Trop.

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Vingt-neuf anticorps monoclonaux (ACM) dirigés contre les souches virales vaccinales RPV-RBOK et RPVL de peste bovine (RPV) et la souche PPRV NIG 75/3 de la peste des petits ruminants (PPRV) ont été caractérisés par radioimmunoprécipitation (RIPA), immunofluorescence ((FI) et immunoenzymologie (ELISA). Vingt-sept d'entre eux étaient dirigés contre la nucléoprotéine (N); deux ACM étaient spécifiques de la protéine de fusion (F) et de la protéine de matrice (M) du virus homologue. Pour ceux qui n'étaient pas précipitants, la réactivité au regard de la protéine de structure était confirmée par (FI et ELISA. La réactivité en (FI de ces ACM a permis de classer des souches RPV et PPRV d'origine géographique différente et de les comparer à deux autres morbillivirus, la rougeole (MV) et la maladie de Carré (CDV). L'ACM dirigé contre la M n'a pas indiqué de variations épitopiques au sein des souches PPRV et l'AcM anti-Fl a délimité un site unique sur l'ensemble des souches RPV et PPRV tout en les distinguant de MV et de CDV. Les ACM anti-N ont été purifiés, biotinylés et analysés par compétition réciproque au regard des souches RPV-RBOK et PPRV-NIG 75/1 utilisées comme antigène de l'ELISA. Ils ont défini sur la nucléoprotéine de ces virus respectivement 6 et 7 sites antigéniques. Sur l'ensemble des sites délimités, certains étaient uniques à RPV (2 sites) et d'autres à PPRV (3 sites). Les ACM qui les reconnaissaient ont permis de distinguer les deux virus sans ambiguïté. Quatre sites se chevauchant sur les virus RPV et PPRV étaient conservés sur l'ensemble des morbillivirus et les sites restants étaient communs à 2 morbillivirus au moins. Trois ACM caractérisés dans cette étude sont de bons candidats pour des tests de diagnostic différentiel.

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Preparation and characterization of monoclonal antibodies to nucleocapsid protein N and H glycoprotein of rinderpest virus

Cited by 14 publications

References 22 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

Mapping of B-Cell Epitopes of Hemagglutinin Protein of Rinderpest Virus

Caractérisation d'anticorps monoclonaux dirigés contre les virus de la peste bovine et de la peste des petits ruminants : identification d'épitopes conservés ou de spécificité stricte sur la nucléoprotéine

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