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Updated: Feb 28, 2026
Analysis of Epididymal Protein Synthesis and Secretion
Published on: August 25, 2018
Secretory expression of a novel human spermatozoa antigen in E. coli and its application to a protein chip
Ming-Zhu Wang1, Zhuo-Lin Qiu2, Xiang-Sheng Cai1
1Institute of Antibody Engineering, School of Laboratory Medical and Biotechnology, Southern Medical University, Guangzhou, People's Republic of China.
Objective:
To produce a recombinant spermatozoa antigen peptide using the E. coli: PhoA system on a protein chip for screening anti-sperm antibodies (ASA).
Results:
The purity of the recombinant spermatozoa antigen exceeded 95% after two-step purification, as assessed using SDS-PAGE and HPLC. The diagnostic performance of a protein chip coated with the recombinant antigen peptide was evaluated by examining ASA in 51 infertile patients in comparison with a commercial ELISA kit. The area under the receiver operating characteristic curve (AUC) was 0.944, which indicated that the protein chip coated with recombinant spermatozoa antigen peptide was consistent with ELISA for ASA detection.
Conclusion:
A recombinant spermatozoa antigen was expressed in the E. coli PhoA secretory expression system and its potential application for clinical ASA detection was validated.
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