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Cystatin 11: A New Member of the Cystatin Type 2 Family

Departments of Pediatrics (K.G.H., Q.L., S.Y., F.S.F., S.H.H.) and Cell and Developmental Biology (P.S., G.G., R.T.R., M.G.O., P.P.) and the Laboratories for Reproductive Biology (K.G.H., Q.L., P.S., G.G., R.S., R.T.R., M.G.O., P.P., F.S.F., S.H.H.), University of North Carolina School of Medicine, Chapel Hill, North Carolina 27599; and the State Key Laboratory of Molecular Biology (Q.L., Y.-L.Z.), Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, Shanghai 200031, China

Address all correspondence and requests for reprints to: Susan H. Hall, Laboratories for Reproductive Biology, CB#7500, University of North Carolina, Chapel Hill, North Carolina 27599. E-mail: . shh{at}med.unc.edu

Cystatin (CST)11, a novel member of the CST type 2 family of cysteine protease inhibitors, was identified in Macaca mulatta epididymis by subtractive hybridization cloning. The human CST11 gene on chromosome 20p11.2 is located near three other CST genes expressed predominantly in the male reproductive tract. The CST11 gene spans three exons, a structure similar to that of other CST family 2 genes. An exon 2-deleted alternative transcript (CST112) was also identified. CST11 mRNA is expressed only in the epididymis as judged by Northern blot hybridization and is androgen regulated. The protein is most abundant in the initial segment, but is detected throughout the epididymis and on ejaculated human sperm. The calculated tertiary structure of CST11 reveals that the three regions corresponding to the protease inhibitory wedge of CST3 are similarly juxtaposed in CST11, consistent with protease inhibitor function. Intact and exon 2-deleted CST11 recombinant proteins were tested for antibacterial activity. After a 2-h incubation of Escherichia coli with 50 µg/ml recombinant CST11 or CST112, bacterial colony-forming units were reduced to 30% of control, indicating that both forms have antimicrobial activity.

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