Conformation and immunogenicity of engineered repeating segment of the circumsporozoite surface protein of Plasmodium falciparum.
Peptide vaccines based on units of the immunodominant tetrapeptide repeats, Asn-Ala-Asn-Pro and Asn-Val-Asp-Pro, of the circumsporozoite surface protein of the parasite Plasmodium falciparum are presently being developed as potential malaria vaccines. The N-terminal fusion of a hydrophobic protein to units of the tetrapeptide repeat affected the immunogenicity and conformational stability of the peptide, and also induced a secondary structure in the peptide. Peptide antigenicity, as well as conformational stability, was significantly increased.
Armah
G E
GE
Faculty of Pharmaceutical Sciences, Osaka University, Japan.
Nishikawa
S
S
Miki
S
S
Omata
Y
Y
Nakabayashi
T
T
Tomita
K
K
D000595:Amino Acid Sequence; D000818:Animals; D000953:Antigens, Protozoan / Q000235:genetics / Q000276:immunology*; D002942:Circular Dichroism; D007114:Immunization; D051379:Mice; D008810:Mice, Inbred C57BL; D008969:Molecular Sequence Data; D010963:Plasmodium falciparum / Q000276:immunology*; D011487:Protein Conformation; D015800:Protozoan Proteins / Q000235:genetics / Q000276:immunology*; D011993:Recombinant Fusion Proteins / Q000276:immunology; D013002:Somatomedins / Q000235:genetics
D000953:Antigens, Protozoan; D015800:Protozoan Proteins; D011993:Recombinant Fusion Proteins; D013002:Somatomedins; C041595:circumsporozoite protein, Protozoan