Vaccine potentials of an intrinsically unstructured fragment derived from the blood stage associated P. falciparum protein PFF0165c. - Related Articles
Vaccine potentials of an intrinsically unstructured fragment derived from the blood stage associated P. falciparum protein PFF0165c.
Infect Immun. 2009 Sep 28;
Authors: Olugbile S, Kulangara C, Bang G, Bertholet S, Suzarte E, Villard V, Frank G, Audran R, Razaname A, Nebie I, Awobusuyi O, Spertini F, Kajava AV, Felger I, Druilhe P, Corradin G
We have identified new malaria vaccine candidates through the combination of bioinformatics prediction of stable protein domains in the Plasmodium falciparum genome, chemical syntheses 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 of such segments (P27A) was well recognized by sera and peripheral blood mononuclear cells of adults living in different malaria-endemic regions. 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, distinct bands in Western blots and are inhibitory in in vitro parasite growth ADCI assay. The immunological properties of P27A together with its low polymorphism and association with clinical protection from malaria in human warrant its further development as a malaria vaccine candidate.
PMID: 19786562 [PubMed - as supplied by publisher] [PubMed-Malaria]