Description
Parasitic nematodes cause serious diseases in animals, humans and plants. Chemoprophylaxis offers short-term benefits, but due to rapid development of drug resistance in parasites there is a pressing need for novel treatments of nematode infection. Parasitic nematodes secrete a structurally novel class of fatty acid and retinol binding (FAR) protein into the surrounding tissues of the host. These proteins are of interest because they may play an important role in scavenging fatty acids and retinoid from the host that are essential for the survival of the parasite and also because the localised depletion of such lipids may have immunomodulatory affects that compromise the host immune response. The genome of the free-living nematode Caenorhabditis elegans encodes eight FAR proteins (Ce-FAR-1 to 8) these fall into three discrete groups as indicated by phylogenetic sequence comparisons and intron positions, the proteins from parasitic nematodes falling into group A. The study describes the successful expression, purification, crystallization and bioinformatics based structure predication of recombinant Ce-FAR-1. The expression of recombinant Ce-FAR-1 was carried out in competent Escherichia coli cells, purification by metal ion affinity chromatography and size exclusion chromatography. The purified Ce-FAR-1 has been crystallized and cryo-protected with and without glycerol (v/v) for X-ray diffraction followed by bioinformatics based structure predication.| Period | 2010 |
|---|---|
| Event title | FEBS Sweden |
| Event type | Conference |
| Degree of Recognition | International |