Towards a Taenia solium cysticercosis vaccine: an epitope shared by Taenia crassiceps and Taenia solium protects mice against experimental cysticercosis.
The Taenia crassiceps recombinant antigen KETc7 has been shown to be effective as a vaccine against experimental murine cysticercosis, a laboratory model used to test potentially promising molecules against porcine Taenia solium cysticercosis. Based on the deduced amino acid sequence of this proline-rich polypeptide, three fragments, GK-1, GK-2, and GK-3, were chemically synthesized in linear form. Of the three peptides, only GK-1 induced sterile protection against T. crassiceps cysticercosis in 40 to 70% of BALB/cAnN male mice. GK-1 is an 18-amino-acid peptide which contains at least one B-cell epitope, as demonstrated by its ability to induce an antibody response to the peptide and T. crassiceps antigen without need of a carrier protein. Immunofluorescence studies revealed that anti-GK1 antibodies strongly react with the native protein in the tegument of T. crassiceps and also with anatomical structures of T. solium eggs, oncospheres, cysticercus, and tapeworm. GK-1 also contains at least one T-cell epitope, capable of stimulating the proliferation of CD8(+) and to a lower extent CD4(+) T cells primed either with the free peptide or T. crassiceps total antigen. The supernatant of the stimulated cells contained high levels of gamma interferon and low levels of interleukin-4. Similar results were obtained with T cells tested for intracellular cytokine production, an indication of the peptide's capacity to induce an inflammatory response. The remarkable protection induced by GK-1 immunization, its physicochemical properties, and its presence in all developmental stages of T. solium point to this synthetic peptide as a strong candidate in the construction of a synthetic vaccine against T. solium pig cysticercosis.
Toledo
A
A
Department of Immunology, Instituto de Investigaciones Biomédicas, UNAM, México D.F. 04510, México.
Larralde
C
C
Fragoso
G
G
Gevorkian
G
G
Manoutcharian
K
K
Hernández
M
M
Acero
G
G
Rosas
G
G
López-Casillas
F
F
Garfias
C K
CK
Vázquez
R
R
Terrazas
I
I
Sciutto
E
E
D000595:Amino Acid Sequence; D000818:Animals; D000909:Antibodies, Helminth / Q000097:blood; D000947:Antigens, Helminth / Q000737:chemistry / Q000235:genetics; D001402:B-Lymphocytes / Q000276:immunology; D003551:Cysticercosis / Q000276:immunology* / Q000517:prevention & control*; D000939:Epitopes / Q000737:chemistry / Q000235:genetics; D015801:Helminth Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology; D007114:Immunization; D007371:Interferon-gamma / Q000096:biosynthesis; D015847:Interleukin-4 / Q000096:biosynthesis; D008213:Lymphocyte Activation; D008297:Male; D051379:Mice; D008807:Mice, Inbred BALB C; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology; D013045:Species Specificity; D013601:T-Lymphocytes / Q000276:immunology; D013621:Taenia / Q000235:genetics / Q000276:immunology*; D014614:Vaccines, Synthetic / Q000235:genetics / Q000276:immunology / Q000494:pharmacology*
D000909:Antibodies, Helminth; D000947:Antigens, Helminth; D000939:Epitopes; D015801:Helminth Proteins; D011994:Recombinant Proteins; D014614:Vaccines, Synthetic; D015847:Interleukin-4; D007371:Interferon-gamma