Crystallization and preliminary structural analysis of an antibody complex formed with PfMSP1-19, a malaria vaccine candidate

Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1246-8. doi: 10.1107/s0907444902007667. Epub 2002 Jun 20.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal / chemistry
  • Antigen-Antibody Complex / chemistry*
  • Dimerization
  • Epidermal Growth Factor / chemistry
  • Epitopes
  • Malaria Vaccines / chemistry*
  • Mice
  • Plasmodium falciparum / chemistry*
  • Protein Structure, Tertiary
  • X-Ray Diffraction / methods*

Substances

  • Antibodies, Monoclonal
  • Antigen-Antibody Complex
  • Epitopes
  • Malaria Vaccines
  • Epidermal Growth Factor