Immunological Data Discovery Index
Immunological Data Discovery Index
| authorizations: |
registration not required
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| accessURL: |
http://www.iedb.org/reference/1007641 |
| landingPage: |
http://www.iedb.org/assay/1474411 |
| type: |
Literature
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| publicationVenue: |
PLoS One
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| dates: |
2007
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| study type: | b cell assays |
| subject species: |
| fullName: |
Shinji L Okitsu
Olivier Silvie
Nicole Westerfeld
Marija Curcic
Andreas R Kammer
Markus S Mueller
Robert W Sauerwein
John A Robinson
Blaise Genton
Dominique Mazier
Rinaldo Zurbriggen
Gerd Pluschke
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| method: |
ELISA
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| name: |
A virosomal malaria peptide vaccine elicits a long-lasting sporozoite-inhibitory antibody response in a phase 1a clinical trial.
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| description: |
The authors synthesized a cyclic mimotopic peptide based on the NPNA-repeat region of CSP from P. falciparum. The peptides folded conformation comes from cross-linking of an amino group at the beta position of Pro at position 6 to the spatially adjacent side-chain carboxyl of Glu, which replaces Ala at position 16. This peptide was designed to optimize both synthesis and immunogenicity.
After two immunizations, all volunteers receiving the virosomally-formulated UK-39 alone (10ug or 50ug) or UK-39 plus AMA49-C1 (50ug) had developed anti-epitope UK-39 IgG response above an endpoint titer of 400 and 600, respectively. In a separate assay, the avidity of anti-UK-39 IgG was measured using elution ELISAs with chaotrophic salt. The mean avidity of the vaccine-induced avidity increased by two-fold to approximately 1M in all groups over the course of immunization with the epitope-virosome preparation. There was no difference between the 10ug and 50ug epitope concentration. Formulating the vaccine with another peptide, AMA49-C1, did not negatively affect immunogenicity.
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| name: |
iedb
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| homePage: |
http://www.iedb.org |
