Crystallization and preliminary structural analysis of an antibody complex formed with PfMSP1-19, a malaria vaccine candidate.
The 11 kDa C-terminal fragment of the proteolyticly matured surface antigen, PfMSP1, from Plasmodium falciparum is a promising malaria vaccine candidate. The soluble recombinant form of this naturally occurring fragment has been crystallized as a complex with the Fab of a specific murine monoclonal antibody. The crystals belong to the space group P2(1), with unit-cell parameters a = 51.8, b = 213.5,c = 60.0 A, beta =101.0 degrees, and with Z = 4. Diffraction data have been measured to 2.9 A resolution and a preliminary model of the complex has been determined by molecular replacement. The epitope recognised by G17.12 is located on the N-terminal EGF-like domain of the antigen.
Pizarro
J C
JC
Unité d'Immunologie Structurale, CNRS URA 2185, Institut Pasteur, 25 Rue du Dr Roux, 75724 Paris, France.
Chitarra
V
V
Calvet
C
C
Verger
D
D
Bentley
G A
GA
D000818:Animals; D000911:Antibodies, Monoclonal / Q000737:chemistry; D000936:Antigen-Antibody Complex / Q000737:chemistry*; D019281:Dimerization; D004815:Epidermal Growth Factor / Q000737:chemistry; D000939:Epitopes; D017780:Malaria Vaccines / Q000737:chemistry*; D051379:Mice; D010963:Plasmodium falciparum / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D014961:X-Ray Diffraction / Q000379:methods*
D000911:Antibodies, Monoclonal; D000936:Antigen-Antibody Complex; D000939:Epitopes; D017780:Malaria Vaccines; D004815:Epidermal Growth Factor