Extraction of Candida Albicans Cell Wall Mannoprotein

Mannoproteins of candida albicans cell wall with their considerable impact on immune system re of importance, Various studies have focused on the purification and characterization of these proteins. Different approaches including the wage of tritonx-lOO (2% Vo1.No1.), deoxycholate sodium (Doc), 5mM EDTA, 6 molar urea Zymolias to SDS (2% wt.N01.) have been used to xtract and purify mannoproteins. Based on the results of these studies, 2% SDS has been ecognized as the time saving and the best approach in terms ofthe concentration ofprotein btained. Therefore, this method was used in this study. Later, in order to evaluate the natural orm ofmannoprotein, NativePAGE was used which identified the unique band ofthe manroprotein. Applying the SDS-PAGE on this protein, identified molecules having a 22 bands olecular weight (m.w) of 10.5 to 168 KDa. To better purify mannoprotein the affinity hromatography (Con-A) was used which identified proteins with molecular weights of 16.5, 18.75 and 22.5 KDa. To separate more purified proteins, the Anion-exchange chromatography was used which identified proteins with a molecular weight of 22.5 KDa, Mannoprotein has important roles in antigenic complex of cell wall of C.albicans, It is also responsible for immunosuppressive effects of C. Albicans. Therefore having a purified protein in hand, can further help to assess it's effects on the immune system, On the other hand, since antigenic differences of various serotypes of C.albican's in relation to mannoprotein and the differences between virulent strain of wild type and standard laboratory-adopted C.albicans is related to the modified mannoprotein structure, antigenic differences can be studied based on differences in primary structure of protein.