Background

Galectins are proteins of the lectin family, which posess carbonhydrate recognition domains binding specifically to β-galactoside sugar residues. In humans, 10 different galectines have been identified, among which is galectin-3.

Galectin-3 has a size of about 31 kDA and is encoded by a single gene, LGALS3. It has many physiological functions, such as cell adhesion, cell growth and differentiation, and contributes to the development of cancer, inflammation, fibrosis and others.

Idea

The specific binding of galectin-3 enables the construction of a detetcion system. Parts of the lipopolysaccharide structure (LPS) of Pseudomonas aeruginosa can be bound by galectin-3. A fusion protein of galectin-3 and a reporter protein, such as a fluorescent protein, can be built with which Pseudomonas aeruginosa can be detected.

Aims

A galectin-3-RFP fusion protein is built and expressed. A his-tag and a snap-tag for purification are included.

Achievements

The galectin-3 - RFP fusion protein part was successfully built and transformed into ... . The cells were cultivated in a ferementation during which the fusion protein was expressed. Subsequently, the fusion protein was purified using the binding of the his-tag to a nickel NTA column.

The fusion protein showed a red fluorescence.

References