Purification, crystallization and X-ray diffraction analysis of Trypanosoma congolense insect-stage surface antigen (TcCISSA)

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Dec 1;68(Pt 12):1503-6. doi: 10.1107/S1744309112042686. Epub 2012 Nov 14.

Abstract

Trypanosoma congolense is a major contributor to the vast socioeconomic devastation in sub-Saharan Africa caused by animal African trypanosomiasis. These protozoan parasites are transmitted between mammalian hosts by tsetse-fly vectors. A lack of understanding of the molecular basis of tsetse-trypanosome interactions stands as a barrier to the development of improved control strategies. Recently, a stage-specific T. congolense protein, T. congolense insect-stage surface antigen (TcCISSA), was identified that shows considerable sequence identity (>60%) to a previously identified T. brucei insect-stage surface molecule that plays a role in the maturation of infections. TcCISSA has multiple di-amino-acid and tri-amino-acid repeats in its extracellular domain, making it an especially interesting structure-function target. The predicted mature extracellular domain of TcCISSA was produced by recombinant DNA techniques, purified from Escherichia coli, crystallized and subjected to X-ray diffraction analysis; the data were processed to 2.7 Å resolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antigens, Surface / chemistry*
  • Antigens, Surface / isolation & purification*
  • Crystallization
  • Crystallography, X-Ray
  • Insect Vectors / metabolism
  • Protozoan Proteins / chemistry*
  • Protozoan Proteins / isolation & purification*
  • Trypanosoma congolense / immunology*
  • Trypanosomiasis, African / immunology
  • X-Ray Diffraction

Substances

  • Antigens, Surface
  • Protozoan Proteins