Nature 323, 259 - 262 (18 September 1986); doi:10.1038/323259a0

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

William E. Collins^*, Robin F. Anders^†, Marguerite Pappaioanou^*, Gary H. Campbell^*, Graham V. Brown^†, David J. Kemp^†, Ross L. Coppel^†, Jimmie C. Skinner^*, Patricia M. Andrysiak^*, Jenny M. Favaloro^†, Lynn M. Corcoran^†, J. Roger Broderson^*, Graham F. Mitchell^† & Carlos C. Campbell^*

^*Division of Parasitic Diseases and Office of Scientific Services, Center for Infectious Diseases, Centers for Disease Control, US Public Health Service, Atlanta, Georgia 30333, USA
^†The Walter and Elisa Hall Institute of Medical Research, Melbourne, Victoria 3050, Australia

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 invasion⁵. 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.

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