Immunization of Aotus monkeys with recombinant proteins of an erythrocyte surface antigen of Plasmodium falciparum

• Published in: Nature (London) 1986-09, Vol.323 (6085), p.259-262
• Main Authors: Collins, William E., Anders, Robin F., Pappaioanou, Marguerite, Campbell, Gary H., Brown, Graham V., Kemp, David J., Coppel, Ross L., Skinner, Jimmie C., Andrysiak, Patricia M., Favaloro, Jenny M., Corcoran, Lynn M., Broderson, J. Roger, Mitchell, Graham F., Campbell, Carlos C.
• Format: Article
• Language: English
• Subjects: Animals; Antibody Specificity; Antigens, Protozoan - genetics; Antigens, Protozoan - immunology; Antigens, Surface - genetics; Antigens, Surface - immunology; Aotus; Aotus trivirgatus; Applied microbiology; Biological and medical sciences; Biotechnology; Epitopes; Erythrocyte Membrane - immunology; Fundamental and applied biological sciences. Psychology; Health. Pharmaceutical industry; Humanities and Social Sciences; Immunization; Industrial applications and implications. Economical aspects; letter; Microbiology; multidisciplinary; Plasmodium falciparum; Plasmodium falciparum - immunology; Production of active biomolecules; Recombinant Fusion Proteins - immunology; Science; Science (multidisciplinary); Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies (general aspects); Vaccines, Synthetic; Vaccins
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/323259a0

Recent studies have identified and characterized a ring-infected erythrocyte surface antigen (RESA) of the human malaria parasite Plasmodium falciparum with a relative molecular mass ( M r ) of ∼155,000 (refs 1–7). RESA is localized in the micronemes of merozoites and also the membrane of red cells infected with ring-stage parasites. It is thought to be released through the apical pore from the rhoptry at the time of merozoite invasion 5 . Because antibodies directed against this antigen strongly inhibit parasite growth in vitro , RESA may be useful in developing a vaccine against this parasite 4,5,7 Here we describe an immunization trial using Aotus monkeys and Escherichia coli -derived fused polypeptides corresponding to various regions of the RESA molecule. Some monkeys in all test groups, but not in the control group, were protected against overwhelming infection. Strikingly, protection correlated with antibody responses to either of two different repetitive sequences in RESA.