ArticleJournal of virology2002
Identification of immunodominant neutralizing epitopes on the hemagglutinin protein of rinderpest virus.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 20 citations in OpenAlex.
- Identification of a new polymorphism on the wild-type canine distemper virus genome: could this contribute to vaccine failures?Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Article
- Phylogenetic evidence of the intercontinental circulation of a Canine distemper virus lineage in the Americas.Scientific reports · 2019Article
- Phylogenetic analysis of the wild-type strains of canine distemper virus circulating in the United States.Virology journal · 2018Article
- Current perspectives on conventional and novel vaccines against peste des petits ruminants.Veterinary research communications · 2014Article
- Genetic characterization of the Korean LATC06 rinderpest vaccine strain.Virus genes · 2011Article
- Structural basis for the function of anti-idiotypic antibody in immune memory.Molecular immunology · 2009Article
- Identification of a second major site for CD46 binding in the hemagglutinin protein from a laboratory strain of measles virus (MV): potential consequences for wild-type MV infection.Journal of virology · 2002Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The immunodominant epitopes on the hemagglutinin protein of rinderpest virus (RPV-H) were determined by analyzing selected monoclonal antibody (MAb)-resistant mutants and estimating the level of antibody against each epitope in five RPV-infected rabbits with the competitive enzyme-linked immunosorbent assay (c-ELISA). Six neutralizing epitopes were identified, at residues 474 (epitope A), 243 (B), 548 to 551 (D), 587 to 592 (E), 310 to 313 (G), and 383 to 387 (H), from the data on the amino acid substitutions of hemagglutinin protein of MAb-resistant mutants and the reactivities of MAbs against RPV-H to the other morbilliviruses. The epitopes identified in this study are all positioned on the loop of the propeller-like structure in a hypothetical three-dimensional model of RPV-H (J. P. M. Langedijk et al., J. Virol. 71:6155-6167, 1997). Polyclonal sera obtained from five rabbits infected experimentally with RPV were examined by c-ELISA using a biotinylated MAb against each epitope as a competitor. Although these rabbit sera hardly blocked binding of each MAb to epitopes A and B, they moderately blocked binding of each MAb to epitopes G and D and strongly blocked binding of each MAb to epitopes E and H. These results suggest that epitopes at residues 383 to 387 and 587 to 592 may be immunodominant in humoral immunity to RPV infection.
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