Antibody responses stimulated in rabbits, guinea-pigs and mice by recombinant and synthetic portions of a 75 kDa malarial merozoite protein
| Autor: | Pawan Sharma, Robert T. Reese, Sylvia J. Richman |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Immunogen
Guinea Pigs Plasmodium falciparum Protozoan Proteins Antibodies Protozoan Mice Inbred Strains Biology law.invention Guinea pig Mice Species Specificity law Animals Merozoite surface protein General Veterinary General Immunology and Microbiology Immunogenicity Public Health Environmental and Occupational Health biology.organism_classification Virology Molecular biology Recombinant Proteins Infectious Diseases Antigens Surface Humoral immunity Recombinant DNA biology.protein Molecular Medicine Immunization Rabbits Antibody |
| Zdroj: | Vaccine. 10:540-546 |
| ISSN: | 0264-410X |
| DOI: | 10.1016/0264-410x(92)90354-m |
| Popis: | The 75 kDa heat-shock-related protein (p75) of Plasmodium falciparum is an abundant, highly conserved, merozoite surface protein. A bacterial clone, C7, produces a polypeptide (C7Ag) of approximately 30 kDa representing the C-terminal 40% of p75. In several species of animals, the C7Ag stimulated high titre IgG antibodies which cross-react with p75. Two major portions of the C7Ag, theoretically predicted to have strong secondary structural preferences, were modelled with four synthetic peptides. An alpha-helical, hydrophilic region, modelled with a 28-mer, proved a poor immunogen in guinea-pigs and several strains of inbred mice, even though it had been a strong immunogen in rabbits. A disulphide-bonded region of the C7Ag was modelled with three peptides of increasing length, namely 49-, 64- and 76-amino acid residues. In general, the order of immunogenicity was 49 less than 64 less than 76-mer. Antibodies to the 76-mer and the 64-mer reacted strongly with the native parasite protein. The data also suggested that the 76-mer was a good model for the region of the molecule it was made to represent. |
| Databáze: | OpenAIRE |
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