Aim:To express the recombinant peptide from gp52 and pp150 C-terminal peptides of human cytomegalovirus (HCMV) in the Pichia pastoris GS115. Methods: After linearised by Sac Ⅰ or Bgl Ⅱ, respectively, the recombinant plasmids were transformed into Pichia pastoris GS115 by electroporation. The Mut+ and Muts transformants were screened according to their different growth characteristic in MD plates without histidine. Some of positive transformants were confirmed by PCR. All Mut+ and Muts clones were induced with methanol. After 4 days of methanol induction, the dialyzed and lyophilizated products were analyzed by SDS-PAGE and Western blot. Results: Recombinant peptied of HCMV was expressed effectively in Mut+ Pichia pastoris and camp up to 76.5% of total proteins in supernatant. Conclusion: High-level expression of secreted recombinant peptide of HCMV has been successfully archived in Pichia pastoris expression system.