Leukocyte cell-derived chemotaxin 2 (LECT2) is a secretory cytokine that functions in many physiological and
pathological processes. We used a Pichia pastoris
expression system for the recombinant expression of rainbow trout LECT2.
The recombinant LECT2 was purified by UNOsphere S Cation exchange and size-exclusion chromatography columns. The
obtained target protein was highly pure (>96% homogeneity) and the yield was >120 mg/L of yeast cultures. An in vitro
chamber assay revealed that recombinant LECT2 could induce chemotactic responses in rainbow trout head kidney-derived
macrophages. Recombinant LECT2 not only enhanced macrophage respiratory burst activity and bactericidal activity, but also
changed macrophage gene expression. In summary, we established a rapid and efficient method to prepare active recombinant
rainbow trout LECT2 using a yeast expression system and column chromatography. Bioactive recombinant LECT2 is essential
for studies on protein functions.