Volume 55, Issue 6
  • ISSN: 0002-9637
  • E-ISSN: 1476-1645



The circumsporozoite antigen (CS) of the simian malarial parasite consists of tandemly repeated immunodominant peptide units that are variable and may play a role in evading the immune system. To study the immunogenicity of this antigen in the absence of the immunodominant repeats, the entire nonrepetitive region of the antigen was expressed in as two fusion proteins with glutathione-S-transferase (GST) representing the amino terminal (GST-CSN) and the carboxy terminal domains (GST-CSC) of the CS antigen. The immunogenicity of these fusion proteins was studied in rabbits and different strains of mice. Antibody raised against both the CSN and CSC domains in both rabbits and every strain of mice recognized the native protein, as detected by immunofluorescence assay (IFA) using sporozoites. A positive IFA reaction was also obtained with sporozoites using antisera raised against the CSC domain. High titer antisera were raised in rabbits against both the domains, whereas mice showed comparatively low titers. On Western blots, mice showed specific response against the CSC domain. In both rabbits and mice, significant titers of antibodies were raised against region II, which has been shown to be the putative sporozoite binding site for hepatocytes in the case of .


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