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The Major Bactericidal Activity of Human Seminal Plasma Is Zinc-Dependent and Derived from Fragmentation of the Semenogelins¹

Anneli M. L. Edström^*, Johan Malm, Birgitta Frohm, Julie A. Martellini, Aleksander Giwercman, Matthias Mörgelin^*, Alexander M. Cole^2, and Ole E. Sørensen^2,*

^* Division of Infection Medicine, Department of Clinical Sciences, Lund University, Lund, Sweden; Division of Clinical Chemistry, Department of Laboratory Medicine, Malmö University Hospital MAS, Lund University, Malmö, Sweden; Department of Molecular Biology & Microbiology, Burnett School of Biomedical Science, University of Central Florida College of Medicine, Orlando, FL 32816; and Centre of Reproductive Medicine, Malmö University Hospital MAS, Lund University, Malmö, Sweden

One of the major roles of seminal plasma is to provide antimicrobial protection for the spermatozoa in the female reproductive tract. We found that the bactericidal activity of seminal plasma was highest after resolution of the seminal clot and that this antibacterial activity subsequently became greatly diminished. The antibacterial activity was derived from peptides generated by fragmentation of the semenogelins while the semenogelin holoproteins displayed no antibacterial activity. After ejaculation the semenogelin-derived peptides were fragmented to smaller and smaller fragments over time and thereby lost antibacterial activity. This paralleled the loss of antibacterial activity of whole seminal plasma both in vitro and after sexual intercourse. Moreover, the antibacterial activity of the semenogelin-derived peptides generated in seminal plasma was strictly zinc-dependent both at neutral and low pH. These data provide novel roles for the resolution of seminal clots and for the high zinc concentration in human seminal plasma.

The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked advertisement in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ This work was supported by grants from the Novo Nordisk Foundation, The Swedish Research Council, The Alfred Österlund Foundation, Clas Groshinkys Memorial Foundation, The Åke Wiberg Foundation, The Royal Physiographic Society in Lund, The Swedish Medical Society, The Crafoord Foundation, The Harald Jeansson Foundation, and Harald and Greta Jeansson Foundation to O.E.S., and National Institutes of Health Grants AI052017, AI060753 and AI065430 to A.M.C. O.E.S. is a recipient of a research fellowship from the Novo Nordisk Foundation.

² Address correspondence and reprint requests to Dr. Ole E. Sørensen, Lund University, Division of Infection Medicine, Biomedical Center B14, Tornavägen 10, 221 84 Lund, Sweden. E-mail address: Ole_E.Sorensen{at}med.lu.se or Dr. Alexander M. Cole, University of Central Florida College of Medicine, Burnett School of Biomedical Sciences, Department of Molecular Biology & Microbiology, 4000 Central Florida Boulevard, Building 20, Room 236, Orlando, FL 32816. E-mail address: acole{at}mail.ucf.edu

³ Abbreviations used in this paper: Sg, semenogelin; AU, acid urea; PSA, prostate-specific Ag; SLPI, secretory leukocyte protease inhibitor.