Skip Navigation



Hum. Reprod. Advance Access published online on March 13, 2008
Human Reproduction, doi:10.1093/humrep/den084
This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF ) Freely available
Right arrow All Versions of this Article:
23/9/2086    most recent
den084v1
Right arrow Submit a response
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Lin, Y.Q.
Right arrow Articles by Jin, S.H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lin, Y.Q.
Right arrow Articles by Jin, S.H.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2008. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Cloning and identification of a novel sperm binding protein, HEL-75, with antibacterial activity and expressed in the human epididymis

Y.Q. Lin{dagger}, J.Y. Li1,{dagger}, H.Y. Wang, J. Liu, C.L. Zhang, W.T. Wang, J. Liu, N. Li and S.H. Jin

Shandong Research Center of Stem Cell Engineering, Yantai Yu-huang-ding Hospital, No. 20, Yu-huang-ding Dong Road, 264000 Yantai, People’s Republic of China

1 Correspondence address. E-mail: sdscli{at}126.com

BACKGROUND: The HEL-75 protein is a β-defensin that was identified by analyzing a human epididymis cDNA library. Studying its function may not only elucidate the mechanisms of host defense, but may also provide new alternatives for novel therapeutic drugs for reproductive tract infections.

METHODS: The HEL-75 gene was amplified by PCR, and its structure and function were predicted and analyzed with bioinformatics tools. Polyclonal serum was raised against recombinant HEL (rHEL)-75 protein. The gene expression pattern was analyzed with RT–PCR and immunofluorescent staining. Finally, the antimicrobial activity and function during fertilization of HEL-75 were analyzed using a colony-forming unit assay and IVF, respectively.

RESULTS: The human HEL-75 gene is located on chromosome 20p13 and encodes a 95 amino acid protein with a predicted N-terminal signal peptide of 22 amino acids. The protein has six conserved cysteine residues, characteristic of members of the β-defensin superfamily, as well as several potential post-translational modification sites. At the transcriptional level, HEL-75 was expressed in the epididymis and lung, but only in the epididymis at the translational level. Immunofluorescent staining showed that HEL-75 protein bound spermatozoa in the epididymis. RHEL-75 protein could kill Escherichia coli in vitro in a dose- and time-dependent fashion. However, no effect was observed on sperm motility nor fertilization when spermatozoa were blocked with anti-rHEL-75 polyclonal serum.

CONCLUSION: HEL-75 is a new β-defensin expressed in the epididymis and on sperm; it may play an important role in host defense.

Key words: epididymis/β-defensin/HEL-75/antibacterial activity/host defense

{dagger} These authors contributed equally to this work.

Submitted on December 21, 2007; resubmitted on February 5, 2008; accepted on February 22, 2008.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Hum Reprod UpdateHome page
G. A. Cornwall
New insights into epididymal biology and function
Hum. Reprod. Update, March 1, 2009; 15(2): 213 - 227.
[Abstract] [Full Text] [PDF]

Home page
 ReproductionHome page
A. I Yudin, T. L Tollner, C. A Treece, R. Kays, G. N Cherr, J. W Overstreet, and C. L Bevins
{beta}-Defensin 22 is a major component of the mouse sperm glycocalyx
Reproduction, December 1, 2008; 136(6): 753 - 765.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.