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Infect Immun, March 1998, p. 1037-1044, Vol. 66, No. 3
0019-9567/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Antigenicity of Recombinant Proteins Derived from Rhoptry-Associated Protein 1 of Plasmodium falciparum

Peter N. Fonjungo,1 Dietrich Stüber,2 and Jana S. McBride1,*

Institute of Cell, Animal and Population Biology, University of Edinburgh, Edinburgh EH9 3JT, Scotland,1 and Pharma Preclinical Research Department, F. Hoffmann-La Roche Ltd., Basel, Switzerland2

Received 30 June 1997/Returned for modification 12 August 1997/Accepted 3 December 1997

Rhoptry-associated protein 1 (RAP1) of Plasmodium falciparum is a potential component of a malaria vaccine. We have expressed in Escherichia coli eight recombinant RAP1 proteins representing almost the entire sequence of the mature protein and assessed the antigenicity of the proteins by immunization of mice. Antisera to six of the recombinant proteins reacted specifically with parasite-derived RAP1 (PfRAP1), as determined by indirect immunofluorescence and by immunoblotting. These proteins were then used in enzyme-linked immunosorbent assays to evaluate human antibody responses to RAP1 during naturally transmitted infections in The Gambia. Immunoglobulin G (IgG) antibodies specifically reactive with the recombinant RAP1 proteins are directed mostly towards fragments containing the N-terminal sequences of mature PfRAP1. The most N-terminal segment (residues 23 to 175) contains only minor epitopes, while major epitopes are outside this region. Antibodies from malaria patients do not compete for a linear epitope recognized by an inhibitory anti-RAP1 monoclonal antibody. Analysis of IgG subclass distribution shows that human anti-RAP1 antibodies are predominantly IgG1.

* Corresponding author. Mailing address: Institute of Cell, Animal and Population Biology, University of Edinburgh, King's Buildings, West Mains Rd., Edinburgh EH9 3JT, Scotland. Phone: 44 131 650 5494. Fax: 44 131 667 3210. E-mail: JMCBRIDE{at}ed.ac.uk.




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