Folding stability of the kinetoplastid membrane protein‐11 (KMP‐11) from Leishmania infantum

Kinetoplastid membrane protein-11 (KMP-11) is a major component of the cell surface of kinetoplastids, and acts as a potent B- and T-cell immunogen during Leishmania infection. Here we report that the Leishmania infantum KMP-11 secondary structure adopts mainly an α-helical conformation at pH 7.5 and that its urea- and thermally-induced unfolding constitute a fully reversible two-step process. This allows estimation of a half-denaturation temperature of ≈65 °C, a ΔGDH2O at 20 °C of ≈14.63 kJ·mol−1, and an increment of the reaction heat of ≈183.92 kJ·mol−1 and an entropy of ≈543.4 J·mol−1·deg−1, respectively, for the native-denatured equilibrium of the KMP-11 in solution. We also report that the KPM-11 protein is induced to adopt a molten globule state at a pH range between pH 4 and pH 6. As a whole, the stability and the specific features of the denaturing effect induced by changes in pH are similar in KMP-11 to various other lipoproteins.