Vaccines are one of the future strategies to prevent and control malaria [5] , one of the most widespread, pathogenic and deadly parasitic diseases in the world. Immunity is only acquired after successive infections in areas of high and stable malaria transmission [6] . Pregnant women become susceptible to placental malaria (PM) independent of any pre-existing immunity acquired during childhood. Placental malaria can have serious consequences for both mother and child such as maternal and infant anaemia, premature labour, low birth weight, and increased neonatal mortality [7] . However, after successive pregnancies women rapidly acquire immunity to PM, indicating that a vaccine strategy against PM may be feasible [8] . PM is caused by the binding of Plasmodium falciparum infected erythrocytes (IE) to chondroitin sulfate A (CSA) present on placental syncytiotrophoblast cells located in the intervillous space [9, 10] . Placental parasites express on the IE surface VAR2CSA, which is a Plasmodium falciparum Erythrocyte Membrane Protein 1 (PfEMP1) that mediates binding of the IE in the placenta [11, 12] . VAR2CSA is a large (350 kDa) polymorphic protein with six Duffy-binding-like (DBL) domains, which complicates the development of a vaccine. A potential animal model for studying protection induced by immunizations with recombinant domains of PfEMP1 could be chimpanzees (Pan troglodytes), whose natural malaria parasite, Plasmodium reichenowi, is closely related to P. falciparum [13] . However, for ethical and economic reasons this is not a feasible model for malaria vaccinology. To date, most malaria antigens are produced by recombinant technology and tested in lower mammalian species, such as rodents and rabbits. These models have allowed analysis of antibody responses to different combinations and boundaries of the six DBL-domains of VAR2CSA. Initially, we expressed all DBL-domains fromVAR2CSA-3D7 and found that all domains except DBL4e, could induce antibodies against native VAR2CSA expressed on the surface of IE, with limited differences in immunizations of mice and rabbits [14] . However, these VAR2CSA-3D7 specific sera did not show significant inhibition of IE binding to CSA (unpublished data). Recently, in a large screening of the immunogenicity of different VAR2CSA antigens from the parasite line FCR3 using rat immunizations, we found that the DBL4e domain of VAR2CSA could elicit the desired adhesion-inhibitory antibodies [15] . However, the induction of functional inhibitory antibodies to certain DBL-domains is poorly reproducible and the immune response tends to focus on non-adhesion blocking epitopes [16, 17] . In addition higher levels of inhibitory antibodies are acquired using full-length VAR2CSA (FV2) as compared to single DBLdomains [18] . To further investigate the induction of adhesion blocking antibody responses, all single recombinant domains of VAR2CSA-FCR3 were used in immunizations of mice, rats and rabbits, and compared to responses raised against the full length recombinant protein.