Open AccessPurification, crystallization and X‐ray diffraction analysis of Trypanosoma congolense insect‐stage surface antigen ( Tc CISSA)
Author(s) -
Tonkin Michelle L.,
Workman Sean D.,
Eyford Brett A.,
Loveless Bianca C.,
Fudge Jessica L.,
Pearson Terry W.,
Boulanger Martin J.
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112042686
Subject(s) - trypanosoma , biology , trypanosoma brucei , recombinant dna , antigen , extracellular , peptide sequence , biochemistry , genetics , gene
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 ( Tc CISSA), 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. Tc CISSA 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 Tc CISSA 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.