Please use this identifier to cite or link to this item: http://hdl.handle.net/123456789/3813
Title: Characterization of conserved T- and B-cell epitopes in plasmodium falciparum major merozoite surface protein 1
Authors: Parra, M.
Hui, G.
Johnson, A.H.
Berzofsky, J.A.
Roberts, T.
Quakyi, I.A.
Taylor, D.W.
Keywords: EMTREE drug terms: amino acid; antibody; epitope; merozoite surface protein 1; vaccine
EMTREE medical terms: animal cell; antibody production; antibody response; article; B lymphocyte; enzyme linked immunosorbent assay; immunization; immunogenicity; lymphocyte proliferation; mouse; nonhuman; Plasmodium falciparum; priority journal; T lymphocyte
MeSH: Amino Acid Sequence; Animals; Antibodies, Protozoan; Cell Division; Conserved Sequence; Epitope Mapping; Epitopes, B-Lymphocyte; Epitopes, T-Lymphocyte; Female; H-2 Antigens; Humans; Merozoite Surface Protein 1; Mice; Mice, Inbred BALB C; Mice, Inbred C57BL; Molecular Sequence Data; Peptides; Plasmodium falciparum; Protozoan Vaccines; T-Lymphocytes; Vaccination; Vaccines, Synthetic
Issue Date: 2000
Publisher: Infection and Immunity
Citation: Parra, M., Hui, G., Johnson, A. H., Berzofsky, J. A., Roberts, T., Quakyi, I. A., & Taylor, D. W. (2000). Characterization of conserved T- and B-cell epitopes in plasmodium falciparum major merozoite surface protein 1. Infection and Immunity, 68(5), 2685-2691.
Abstract: Vaccines for P. falciparum will need to contain both T, and B-cell epitopes. Conserved epitopes are the most desirable, but they are often poorly immunogenic. The major merozoite surface protein 1 (MSP-1) is currently a leading vaccine candidate antigen. In this study, six peptides from conserved or partly conserved regions of MSP-1 were evaluated for immunogenicity in B10 congenic mice. Following immunization with the peptides, murine T cells were tested for the ability to proliferate in vitro and antibody responses to MSP-1 were evaluated in vivo. The results showed that one highly conserved sequence (MSP-11, VTHESYQELVKKLEALEDAV; located at amino acid positions 20 to 39) and one partly conserved sequence (MSP-123, GLFHKEKMIL NEEEITTKGA; located at positions 44 to 63) contained both T- and B-cell epitopes. Immunization of mice with these peptides resulted in T-cell proliferation and enhanced production of antibody to MSP-1 upon exposure to merozoites. MSP-11 stimulated T-cell responses in three of the six strains of mice evaluated, whereas MSP-123 was immunogenic in only one strain. Immunization with the other four peptides resulted in T-cell responses to the peptides, but none of the resulting peptide-specific T cells recognized native MSP-1. These results demonstrate that two sequences located in the N terminus of MSP-1 can induce T- and B-cell responses following immunization in a murine model. Clearly, these sequences merit further consideration for inclusion in a vaccine for malaria.
URI: http://hdl.handle.net/123456789/3813
ISSN: 00199567
Appears in Collections:School of Public Health 9

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