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Infection and Immunity, December 2009, p. 5701-5709, Vol. 77, No. 12
0019-9567/09/$08.00+0     doi:10.1128/IAI.00652-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Vaccine Potentials of an Intrinsically Unstructured Fragment Derived from the Blood Stage-Associated Plasmodium falciparum Protein PFF0165c{triangledown}

S. Olugbile,1 C. Kulangara,2 G. Bang,3 S. Bertholet,4 E. Suzarte,5 V. Villard,5 G. Frank,5 R. Audran,1 A. Razaname,5 I. Nebie,6 O. Awobusuyi,7 F. Spertini,1 A. V. Kajava,8 I. Felger,2 P. Druilhe,3 and G. Corradin5*

Centre Hospitalier Universitaire Vaudois CHUV, Lausanne, Switzerland,1 Swiss Tropical Institute, Basel, Switzerland,2 Pasteur Institute, Paris, France,3 Infectious Disease Research Institute, Seattle, Washington,4 Biochemistry Department, University of Lausanne, Epalinges, Switzerland,5 Centre National de Recherche et de Formation sur le Paludisme, Ouagadougou, Burkina Faso,6 Lagos State University Teaching Hospital, Lagos, Nigeria,7 CRBM, CNRS, University of Montpellier, Montpellier, France8

Received 9 June 2009/ Returned for modification 19 July 2009/ Accepted 16 September 2009

We have identified new malaria vaccine candidates through the combination of bioinformatics prediction of stable protein domains in the Plasmodium falciparum genome, chemical synthesis of polypeptides, in vitro biological functional assays, and association of an antigen-specific antibody response with protection against clinical malaria. Within the predicted open reading frame of P. falciparum hypothetical protein PFF0165c, several segments with low hydrophobic amino acid content, which are likely to be intrinsically unstructured, were identified. The synthetic peptide corresponding to one such segment (P27A) was well recognized by sera and peripheral blood mononuclear cells of adults living in different regions where malaria is endemic. High antibody titers were induced in different strains of mice and in rabbits immunized with the polypeptide formulated with different adjuvants. These antibodies recognized native epitopes in P. falciparum-infected erythrocytes, formed distinct bands in Western blots, and were inhibitory in an in vitro antibody-dependent cellular inhibition parasite-growth assay. The immunological properties of P27A, together with its low polymorphism and association with clinical protection from malaria in humans, warrant its further development as a malaria vaccine candidate.

* Corresponding author. Mailing address: Biochemistry Department, University of Lausanne, 1066 Epalinges, Switzerland. Phone: 41 21 692 5731. Fax: 41 21 6925705. E-mail: giampietro.corradin{at}unil.ch

{triangledown} Published ahead of print on 28 September 2009.

Editor: W. A. Petri, Jr.

Infection and Immunity, December 2009, p. 5701-5709, Vol. 77, No. 12
0019-9567/09/$08.00+0     doi:10.1128/IAI.00652-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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